Journal articles: 'CHAPS'

1

Currey, John. "Clever chaps." Nature 343, no. 6255 (January 1990): 226. http://dx.doi.org/10.1038/343226a0.

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Sogo, Yu, Daiki Yokoyama, Atsuo Ito, Atsushi Yamazaki, and Racquel Z. LeGeros. "F-Substituted Carbonate Apatite for Promoting Bone Formation." Key Engineering Materials 309-311 (May 2006): 141–44. http://dx.doi.org/10.4028/www.scientific.net/kem.309-311.141.

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Abstract. Fluoride (F-)-substituted type-B carbonate-containing hydroxyapatites (CHAPs) were prepared as bone substitutes with a F-releasing ability. The F- contents in the F-substituted CHAPs were 16-22 times larger than that in normal adult human bones. The carbonate contents in the F-substituted CHAPs corresponded to that in human bones. The F-substituted CHAPs released F- in an acetic acid – sodium acetate buffer at pH 4.9; within only 3 h, the F- concentration in the buffer increased to more than 63.9 µg L-1, which was 1.5~8.9 times higher than that in a body fluid of normal adult humans. Although the F- concentration rapidly decreased probably due to the precipitation of a certain phase containing F-, the F-substituted CHAPs exhibited the ability to increase the F- concentration in a body fluid by bone resorption. Therefore, it is expected that the F-substituted CHAPs will be feasible as a F-releasing material for promoting bone formation.

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3

BESSENGER, SUZANNE. "We Homes Chaps." Visual Anthropology Review 20, no. 1 (April 2004): 96–97. http://dx.doi.org/10.1525/var.2004.20.1.96.

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4

Sakai, S., F. Ike, K. Kohmoto, and T. Johke. "Separation of rabbit mammary-gland prolactin receptors by ion-exchange chromatography, h.p.l.c.-gel filtration and ultracentrifugation." Biochemical Journal 237, no. 3 (August 1, 1986): 647–53. http://dx.doi.org/10.1042/bj2370647.

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Rabbit mammary-gland prolactin (Prl) receptors in the microsomal fraction were solubilized in 7.5 mM-Chaps) or 1% Triton X-100 and analysed by ion-exchange chromatography using DEAE-Bio-Gel A. Prl receptors in the presence of 7.5 mM-Chaps were separated into two different fractions (Fr. A and B), both of which showed identical specificity of binding to peptide hormones as those in the Chaps or Triton extract. oPrl and human growth hormone (hGH) bound to the same site, but other non-lactogenic hormones (follicle-stimulating hormone, oGH, luteinizing hormone and insulin) failed to bind to the Prl receptors. The dissociation constant (Kd) for Prl binding to the receptors in Fr. A was about 50% of those in Fr. B, suggesting that the rabbit mammary gland contains two types of Prl receptors, one with a high, and one with a low, Kd for Prl binding. A decrease in the concentration of Chaps in the column buffer to 4 mM caused aggregation of the receptors in Fr. A. H.p.l.c.-gel filtration, using Shim pack 150 and 300 columns connected in series, separated the receptor as a protein with an Mr of 74,000 +/- 4,900 (mean +/- S.D.) in the presence of 5 mM-Chaps, or of 36,800 +/- 2,100 in the presence of 7.5 mM-Chaps. Sucrose-gradient-centrifugation analysis showed that the Prl-receptor complexes in the presence of 5 mM-Chaps were sedimented between gamma-globulin and bovine serum albumin (5.56 +/- 0.22 S). As the Chaps concentration was increased to 7.5 mM, a further peak of the Prl-receptor complexes (4.01 +/- 0.23 S) appeared below ovalbumin. The present data suggest that the binding subunit causes the monomeric subunit to aggregate with itself or with another specific associated protein of similar Mr.

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Cladera, Josep, Jean-Louis Ricaud, Joaquim Villa Verde, and Mireia DuNach. "Liposome Solubilization and Membrane Protein Reconstitution Using Chaps and Chapso." European Journal of Biochemistry 243, no. 3 (February 1997): 798–804. http://dx.doi.org/10.1111/j.1432-1033.1997.00798.x.

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6

Cantor, Geoffrey. "Of maps and chaps." Metascience 23, no. 1 (May 15, 2013): 191–94. http://dx.doi.org/10.1007/s11016-013-9804-4.

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Kolb, F. L., N. J. Smith, C. M. Brown, and L. L. Domier. "Registration of ‘Chaps’ Oat." Crop Science 39, no. 1 (January 1999): 286. http://dx.doi.org/10.2135/cropsci1999.0011183x003900010052x.

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8

Kargaltsev, Oleg, Martin Durant, George G. Pavlov, and Gordon Garmire. "CHANDRA PULSAR SURVEY (ChaPS)." Astrophysical Journal Supplement Series 201, no. 2 (August 1, 2012): 37. http://dx.doi.org/10.1088/0067-0049/201/2/37.

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9

Drummond, D. Allan. "Protein Evolution: Innovative Chaps." Current Biology 19, no. 17 (September 2009): R740—R742. http://dx.doi.org/10.1016/j.cub.2009.07.039.

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Bennett, M. K., N. Calakos, T. Kreiner, and R. H. Scheller. "Synaptic vesicle membrane proteins interact to form a multimeric complex." Journal of Cell Biology 116, no. 3 (February 1, 1992): 761–75. http://dx.doi.org/10.1083/jcb.116.3.761.

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Potential interactions between membrane components of rat brain synaptic vesicles were analyzed by detergent solubilization followed by size fractionation or immunoprecipitation. The behavior of six synaptic vesicle membrane proteins as well as a plasma membrane protein was monitored by Western blotting. Solubilization of synaptic vesicle membranes in CHAPS resulted in the recovery of a large protein complex that included SV2, p65, p38, vesicle-associated membrane protein, and the vacuolar proton pump. Solubilization in octylglucoside resulted in the preservation of interactions between SV2, p38, and rab3A, while solubilization of synaptic vesicles with Triton X-100 resulted in two predominant interactions, one involving p65 and SV2, and the other involving p38 and vesicle-associated membrane protein. The multicomponent complex preserved with CHAPS solubilization was partially reconstituted following octylglucoside solubilization and subsequent dialysis against CHAPS. Reduction of the CHAPS concentration by gel filtration chromatography resulted in increased recovery of the multicomponent complex. Examination of the large complex isolated from CHAPS-solubilized vesicles by negative stain EM revealed structures with multiple globular domains, some of which were specifically labeled with gold-conjugated antibodies directed against p65 and SV2. The protein interactions defined in this report are likely to underlie aspects of neurotransmitter secretion, membrane traffic, and the spatial organization of vesicles within the nerve terminal.

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Haimovich, B., B. J. Aneskievich, and D. Boettiger. "Cellular partitioning of beta-1 integrins and their phosphorylated forms is altered after transformation by Rous sarcoma virus or treatment with cytochalasin D." Cell Regulation 2, no. 4 (April 1991): 271–83. http://dx.doi.org/10.1091/mbc.2.4.271.

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A sequential extraction procedure of 3-[(3-cholamidopropyl)-dimethylammonio]-1-propane sulfonate (CHAPS) buffer followed by RIPA or Laemmli sample buffer was developed to define two distinct subpopulations of beta-1 integrins in primary chicken embryo fibroblasts. Extraction of cells in culture revealed an association of adhesion plaque-localized integrin with the CHAPS-insoluble fraction. Phosphorylated integrins were found in both fractions, but the specific phosphorylation was 12-fold higher in the CHAPS insoluble fraction. The phosphorylation was evenly distributed between phosphoserine and phosphotyrosine. Transformation by Rous sarcoma virus caused a redistribution of integrin to rosettes and an increase in total integrin phosphorylation. Treatment with cytochalasin D caused a redistribution of the adhesion plaque-associated integrin into lacelike structures and reduced the level of integrin phosphorylation. These treatments also caused an altered distribution of phosphorylated integrin between the CHAPS soluble and insoluble fractions. These results suggest a role for integrin phosphorylation in the assembly and disassembly of cellular adhesion structures.

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Rockenbauch, Uli, Alicja M. Ritz, Carlos Sacristan, Cesar Roncero, and Anne Spang. "The complex interactions of Chs5p, the ChAPs, and the cargo Chs3p." Molecular Biology of the Cell 23, no. 22 (November 15, 2012): 4402–15. http://dx.doi.org/10.1091/mbc.e11-12-1015.

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The exomer complex is a putative vesicle coat required for the direct transport of a subset of cargoes from the trans-Golgi network (TGN) to the plasma membrane. Exomer comprises Chs5p and the ChAPs family of proteins (Chs6p, Bud7p, Bch1p, and Bch2p), which are believed to act as cargo receptors. In particular, Chs6p is required for the transport of the chitin synthase Chs3p to the bud neck. However, how the ChAPs associate with Chs5p and recognize cargo is not well understood. Using domain-switch chimeras of Chs6p and Bch2p, we show that four tetratricopeptide repeats (TPRs) are involved in interaction with Chs5p. Because these roles are conserved among the ChAPs, the TPRs are interchangeable among different ChAP proteins. In contrast, the N-terminal and the central parts of the ChAPs contribute to cargo specificity. Although the entire N-terminal domain of Chs6p is required for Chs3p export at all cell cycle stages, the central part seems to predominantly favor Chs3p export in small-budded cells. The cargo Chs3p probably also uses a complex motif for the interaction with Chs6, as the C-terminus of Chs3p interacts with Chs6p and is necessary, but not sufficient, for TGN export.

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13

Jones, Roger. "Splendid chaps, all of them." Nature Physics 10, no. 1 (November 25, 2013): 3–4. http://dx.doi.org/10.1038/nphys2846.

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14

Ramya, R., B. Mohana Subramanian, V. Sivakumar, R. L. Senthilkumar, K. R. S. Sambasiva Rao, and V. A. Srinivasan. "Expression and Solubilization of Insect Cell-Based Rabies Virus Glycoprotein and Assessment of Its Immunogenicity and Protective Efficacy in Mice." Clinical and Vaccine Immunology 18, no. 10 (August 3, 2011): 1673–79. http://dx.doi.org/10.1128/cvi.05258-11.

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ABSTRACTRabies is a fatal zoonotic disease of serious public health and economic significance worldwide. The rabies virus glycoprotein (RVG) has been the major target for subunit vaccine development, since it harbors domains responsible for induction of virus-neutralizing antibodies, infectivity, and neurovirulence. The glycoprotein (G) was cloned using the baculovirus expression vector system (BEVS) and expressed inSpodoptera frugiperda(Sf-9) cells. In order to obtain a soluble form of G suitable for experimentation in mice, 18 different combinations of buffers and detergents were evaluated for their ability to solubilize the insect cell membrane-associated G. The combination that involved 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate (CHAPS) detergent in lysis buffer 1, formulated with Tris, NaCl, 10% dimethyl sulfoxide (DMSO), and EDTA, gave the highest yield of soluble G, as evidenced by the experimental data. Subsequently, several other parameters, such as the concentration of CHAPS and the duration and temperature of the treatment for the effective solubilization of G, were optimized. The CHAPS detergent, buffered at a concentration of 0.4% to 0.7% (wt/vol) at room temperature (23 to 25°C) for 30 min to 1 h using buffer 1, containing 10% DMSO, resulted in consistently high yields. The G solubilized using CHAPS detergent was found to be immunogenic when tested in mice, as evidenced by high virus-neutralizing antibody titers in sera and 100% protection upon virulent intracerebral challenge with the challenge virus standard (CVS) strain of rabies virus. The results of the mice study indicated that G solubilized with CHAPS detergent retained the immunologically relevant domains in the native conformation, thereby paving the way for producing a cell-free and efficacious subunit vaccine.

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Connor, Karen I., Eric M. Cheng, Frances Barry, Hilary C. Siebens, Martin L. Lee, David A. Ganz, Brian S. Mittman, et al. "Randomized trial of care management to improve Parkinson disease care quality." Neurology 92, no. 16 (March 22, 2019): e1831-e1842. http://dx.doi.org/10.1212/wnl.0000000000007324.

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ObjectiveTo test effects on care quality of Chronic Care Model-based Parkinson disease (PD) management.MethodsThis 2-group stratified randomized trial involved 328 veterans with PD in southwestern United States. Guided care management, led by PD nurses, was compared to usual care. Primary outcomes were adherence to 18 PD care quality indicators. Secondary outcomes were patient-centered outcome measures. Data sources were telephone survey and electronic medical record (EMR). Outcomes were analyzed as intent-to-treat comparing initial and final survey and repeated-measures mixed-effects models.ResultsAverage age was 71 years; 97% of participants were male. Mean proportion of participants receiving recommended PD care indicators was significantly higher for the intervention than for usual care (0.77 vs 0.58) (mean difference 0.19, 95% confidence interval [CI] 0.16, 0.22). Of 8 secondary outcomes, the only significant difference of the changes over time was in the positive Patient Health Questionnaire–2 depression screen for intervention minus usual care (−11.52 [95% CI −20.42, −2.62]).ConclusionA nurse-led chronic care management intervention, Care Coordination for Health Promotion and Activities in Parkinson's Disease (CHAPS), substantially increased adherence to PD quality of care indicators among veterans with PD, as documented in the EMR. Of 8 secondary outcomes assessed, a screening measure for depressive symptomatology was the only measure that was better in the intervention compared to usual care. More telephone calls in CHAPS were the only utilization difference over usual care. While CHAPS appears promising for improving PD care, additional iterative research is needed to refine the CHAPS model in routine clinical care so that it measurably improves patient-centered outcomes (NCT01532986).Classification of evidenceThis study provides Class I evidence that for patients with PD, CHAPS increased adherence to PD quality of care indicators.

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Leventouri, Th, B. C. Chakoumakos, N. Papanearchou, and V. Perdikatsis. "Comparison of crystal structure parameters of natural and synthetic apatites from neutron powder diffraction." Journal of Materials Research 16, no. 9 (September 2001): 2600–2606. http://dx.doi.org/10.1557/jmr.2001.0357.

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A systematic behavior in the crystal structure parameters of natural, synthetic, carbonate, and non-carbonate apatite is revealed from Rietveld refinements of neutron powder diffraction experiments. The results of this work on synthetic carbonate hydroxyapatites (CHAps) are consistent with the mechanism of carbonate substitution on the mirror plane of the phosphate tetrahedron, as it was introduced for the natural carbonate fluorapatite (CFAp). The present comparison shows that the tetrahedral bond lengths P–O1 and P–O2 decrease by 3–4% in all carbonate apatites. The atomic displacement parameters (ADPs) of the tetrahedral (T) and the O3 sites are greater in the carbonate than in the non-carbonate apatites. The atomic positional disorder of the T site (P/C site) is greater in the CFAp than in the CHAps, while the opposite happens at the O3 sites. Finally, the room-temperature ADPs of all of the atoms in the CFAp and CHAps show the same behavior as in the corresponding non-carbonate materials.

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17

Giacomelli, Carla E., Arnouldus W. P. Vermeer, and Willem Norde. "Micellization and Adsorption Characteristics of CHAPS." Langmuir 16, no. 11 (May 2000): 4853–58. http://dx.doi.org/10.1021/la9913708.

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18

Kaufman, Kyle. "Chaps: Sara M. Larsen's Doubly Circulatory." American Book Review 27, no. 4 (2006): 18. http://dx.doi.org/10.1353/abr.2006.0143.

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19

Jaroudi, Wael A., Abdo R. Jurjus, Marwan E. El-Sabban, Maud T. Kamal, Khalil M. Bitar, and Anwar B. Bikhazi. "Endothelium and myocyte cellular insulin receptor alterations in a rat model of myocardial infarction." Canadian Journal of Physiology and Pharmacology 81, no. 3 (March 1, 2003): 267–73. http://dx.doi.org/10.1139/y02-157.

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Ischemic heart disease is considered to be one of the leading causes of death in adults. While extensive research on mechanisms contributing to the pathogenesis of myocardial infarction (MI) has been underway, it is not known whether insulin receptor characteristics and postreceptor signaling have been fully addressed as yet. Present work attempts to investigate whether the remodeling process effectively induces alteration(s) in insulin-binding characteristics at the coronary endothelium and cardiomyocytes using a rat heart model of MI. MI was induced by ligation of the left anterior descending coronary artery of adult male SpragueDawley rats. Two animal groups were used in the study: (i) sham-operated CHAPS-untreated and CHAPS-treated, and (ii) MI CHAPS-untreated and MI CHAPS-treated. A physical model describing 1:1 stoichiometry of reversible insulin binding to its receptors present on the endothelium and at cardiomyocytes after CHAPS treatment was considered for data analysis. Quantitation of the collected effluents after heart perfusion, the inlet at the aortic and outlet at the coronary sinus sites, were curve fitted using a first-order Bessel function, which determines the binding constants (kn), the reversible constant (kn), the dissociation constant (kd = kn/kn), and the residency time constant (τ = 1/kn). In addition, hearts were excised, separated into right and left ventricles, and individually weighed, and areas of infarcted regions were measured. Results of the MI group showed significant increases in relative heart mass, left ventricle mass, and right ventricle mass normalized to total body mass. MI induced severe ischemia and irreversible myocardial injury as assessed by planimetry and histologic studies. The data showed differences in insulin receptor affinities at the endothelial and cardiac myocytes in the sham and in the MI-operated rats. The observed reduction in the binding affinity of insulin at the myocyte postinfarction may explain the pathogenic role of insulin in ischemic heart disease and, hence, resistance. Therefore, insulin administration during and post MI might be cardioprotective.Key words: myocardial infarction, insulin binding, cardioprotection, insulin therapy.

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Badour, S. S., and W. K. Kim. "Detection of specific polypeptides in Chlamydomonas segnis adapted to atmospheric concentrations of CO2, using a zwitterionic detergent." Canadian Journal of Botany 66, no. 9 (September 1, 1988): 1750–54. http://dx.doi.org/10.1139/b88-240.

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Polypeptides from 5% CO2 adapted and air-adapted cells of Chlamydomonas segnis, extracted in the presence of the zwitterionic (ampholytic) detergent CHAPS, then lyophilized and washed with a chloroform – methanol mixture, were compared with those extracted in the presence of sodium dodecyl sulphate and Nonidet-P40 and precipitated by cold acetone, using two-dimensional electrophoresis. The electrophoretograms of these detergent-soluble polypeptides indicate that the use of CHAPS instead of sodium dodecyl sulphate – Nonidet-P40 considerably increases the mobility of proteins in the isoelectric focussing gels, improves resolution, and facilitates the detection of polypeptides with low molecular masses on the gradient gels. Comparison of polypeptides extracted with CHAPS from air-adapted and 5% CO2 adapted cells revealed the presence of 20 polypeptides unique to the former type of cells. Fourteen of these polypeptides had molecular masses of approximately 20 kDa and isoelectric-point (pI) values ranging from 7.4 to 6.4. They represented the major proteins characteristic of cells capable of active photosynthesis and growth under atmospheric concentrations of CO2.

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Murayama, Takashi, Toshiharu Oba, Shigeki Kobayashi, Noriaki Ikemoto, and Yasuo Ogawa. "Postulated role of interdomain interactions within the type 1 ryanodine receptor in the low gain of Ca2+-induced Ca2+ release activity of mammalian skeletal muscle sarcoplasmic reticulum." American Journal of Physiology-Cell Physiology 288, no. 6 (June 2005): C1222—C1230. http://dx.doi.org/10.1152/ajpcell.00415.2004.

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Ryanodine receptor (RyR) type 1 (RyR1) exhibits a markedly lower gain of Ca2+-induced Ca2+ release (CICR) activity than RyR type 3 (RyR3) in the sarcoplasmic reticulum (SR) of mammalian skeletal muscle (selective stabilization of the RyR1 channel), and this reduction in the gain is largely eliminated using 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid (CHAPS). We have investigated whether the hypothesized interdomain interactions within RyR1 are involved in the selective stabilization of the channel using [3H]ryanodine binding, single-channel recordings, and Ca2+ release from the SR vesicles. Like CHAPS, domain peptide 4 (DP4, a synthetic peptide corresponding to the Leu2442-Pro2477 region of RyR1), which seems to destabilize the interdomain interactions, markedly stimulated RyR1 but not RyR3. Their activating effects were saturable and nonadditive. Dantrolene, a potent inhibitor of RyR1 used to treat malignant hyperthermia, reversed the effects of DP4 or CHAPS in an identical manner. These findings indicate that RyR1 is activated by DP4 and CHAPS through a common mechanism that is probably mediated by the interdomain interactions. DP4 greatly increased [3H]ryanodine binding to RyR1 with only minor alterations in the sensitivity to endogenous CICR modulators (Ca2+, Mg2+, and adenine nucleotide). However, DP4 sensitized RyR1 four- to six-fold to caffeine in the caffeine-induced Ca2+ release. Thus the gain of CICR activity critically determines the magnitude and threshold of Ca2+ release by drugs such as caffeine. These findings suggest that the low CICR gain of RyR1 is important in normal Ca2+ handling in skeletal muscle and that perturbation of this state may result in muscle diseases such as malignant hyperthermia.

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Matsuki, T., J. M. Beach, R. L. Klindt, and B. R. Duling. "Modification of vascular reactivity by alteration of intimal permeability: effect of TNF-alpha." American Journal of Physiology-Heart and Circulatory Physiology 264, no. 6 (June 1, 1993): H1847—H1853. http://dx.doi.org/10.1152/ajpheart.1993.264.6.h1847.

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We investigated the effects of alterations in intimal permeability on microvascular reactivity to small hydrophilic agents in isolated, cannulated, perfused arterioles (65 +/- 6 microns ID) from hamster cheek pouches. Arterioles are 300-fold less responsive to the hydrophilic alpha 1-agonist, phenylephrine, applied to the lumen than when applied to the adventitia. Luminal treatment with tumor necrosis factor-alpha (TNF-alpha, 0.625 micrograms/ml, 1–2 h) potentiated reactivity to luminally applied phenylephrine, but the treatment did not change reactivity to adventitially applied phenylephrine. Similar results were obtained with a brief treatment with the detergent, 3-[(3-cholamidopropyl)dimethylammonio]-1- propanesulfonate (CHAPS; 0.3%, < 30 s). To confirm that a change in permeability had occurred, we measured the movement across the arteriolar wall of a low-molecular-weight hydrophilic fluorescent molecule, fluorescein, before and after luminal treatment with TNF-alpha or CHAPS. Either TNF-alpha or CHAPS significantly increased the rate of movement of fluorescein across the arteriolar wall. These data suggest that one element in the pathophysiology of TNF-alpha is an increase in arteriolar permeability to small, water-soluble agents, which may modify reactivity to circulating vasoactive substances.

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Paganelli, K. A., A. S. Stern, and P. L. Kilian. "Detergent solubilization of the interleukin 1 receptor." Journal of Immunology 138, no. 7 (April 1, 1987): 2249–53. http://dx.doi.org/10.4049/jimmunol.138.7.2249.

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Abstract Interleukin 1 (IL 1) receptors were solubilized from membranes prepared from murine EL-4 thymoma cells with the zwitterionic detergent 3[(3-cholamidopropyl) dimethylammonio]-1-propanesulfonate (CHAPS). Binding of IL 1 to the solubilized receptor was detected by a polyethylene glycol (PEG) precipitation procedure. Concentrations of CHAPS from 4 to 8 mM were effective in solubilizing the IL 1 receptor. At 10 mM CHAPS, there was some loss in binding activity, whereas 2 mM CHAPS was completely ineffective in solubilizing the receptor. Detergent concentrations of 4 mM were routinely used. The solubilized receptor retains the ability to bind 125I-IL 1 in a specific and saturable manner. Scatchard analysis reveals a single type of high affinity binding site having an apparent dissociation constant (KD) of approximately 1.2 X 10(-10) M. Nearly identical KD values are observed for membrane fractions. There are approximately 400 to 500 fmol receptor/mg protein in the detergent extract, corresponding to a two- to threefold enrichment in the Bmax observed for membranes. There is no loss in receptor activity as determined by complete recovery of the total number of binding sites from membranes after solubilization. Binding kinetics show that apparent steady state for the solubilized receptor is reached after 60 min at 37 degrees C. The binding of 125I-IL 1 is essentially irreversible because relatively little bound ligand can be dissociated from the receptor on the addition of excess unlabeled IL 1 at 37 degrees C. Both human IL 1 alpha and IL 1 beta compete for binding of 125I-IL 1 to the soluble receptor, confirming that IL 1 alpha and IL 1 beta bind to the same receptor. Other recombinant proteins, including interferon-alpha A, interferon-gamma, and interleukin 2 have no inhibitory effect.

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Campos, E. I., and D. Reinberg. "New chaps in the histone chaperone arena." Genes & Development 24, no. 13 (July 1, 2010): 1334–38. http://dx.doi.org/10.1101/gad.1946810.

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Banerjee, Probal, John T. Buse, and Glyn Dawson. "Asymmetric extraction of membrane lipids by CHAPS." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 1044, no. 3 (June 1990): 305–14. http://dx.doi.org/10.1016/0005-2760(90)90074-8.

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Sah, Hongkee, and Kil-Soo Kim. "Improvement of Interfacial Protein Stability by CHAPS." Biotechnology Letters 28, no. 8 (April 2006): 567–70. http://dx.doi.org/10.1007/s10529-006-0016-5.

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Kono, Mitsuhiko, Kenneth G. H. Baldwin, Yabai He, Richard T. White, and Brian J. Orr. "CHAPS: a new precision laser-spectroscopic technique." Journal of the Optical Society of America B 23, no. 6 (June 1, 2006): 1181. http://dx.doi.org/10.1364/josab.23.001181.

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Raoult, D. "Gonorrhea resistance: don’t forget the old chaps." European Journal of Clinical Microbiology & Infectious Diseases 36, no. 12 (September 15, 2017): 2537. http://dx.doi.org/10.1007/s10096-017-3099-0.

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Triki, S., J. Ben Hamida, and P. Mazliak. "Diacylglycerol acyltransferase in maturing sunflower seeds." Biochemical Society Transactions 28, no. 6 (December 1, 2000): 689–92. http://dx.doi.org/10.1042/bst0280689.

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Developing sunflower seeds exhibit a high diacylglycerol acyltransferase (DAGAT, EC 2.3.1.20) activity. The distribution of the enzyme has been studied in subcellular fractions prepared by differential centrifugation of seed homogenate. Its activity was characterized using [1-14C]oleoyl-CoA and diolein dispersed in Tween 20. Some properties of the microsomal fraction of DAGAT were investigated. Hyperbolic kinetics were observed, the apparent Km was 60 μM and the specific activity of the reaction 15 pmol/min/mg of protein. Addition of BSA (0.1%) stimulated oleate incorporation, which was not dependent on the presence of exogenous diacylglycerol. Detergents which might solubilize DAGAT, Triton X-100 and CHAPS, were tested for enzyme inhibition, and CHAPS was found to be the least denaturing.

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Bahri, S. "Lipase activity in germinating sunflower seedlings." Biochemical Society Transactions 28, no. 6 (December 1, 2000): 771–73. http://dx.doi.org/10.1042/bst0280771.

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Studying lipase in germinating sunflower seedlings, we looked for an activator of the lipolytic activity. In the presence of 1.25 mM ATP, the enzyme activity increased 2-fold. Lipid-body lipase solubilization was realized using two detergents: Tween 80 and CHAPS. Lipolytic activity was increased 10-fold in the presence of 2% (w/v) CHAPS, showing the probable ‘complexity’ of the enzyme. Looking for the possible lipolytic activity of the 10000g pellet we detected the presence of the enzyme. The pellet extract was mixed, in a range of concentrations, with the oilbody fraction. The resulting lipolytic activity was 4-fold higher. These results give clues as to the subcellular distribution of lipase and its intracellular transport.

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Georgoussi, Z., G. Milligan, and C. Zioudrou. "Immunoprecipitation of opioid receptor-Go-protein complexes using specific GTP-binding-protein antisera." Biochemical Journal 306, no. 1 (February 15, 1995): 71–75. http://dx.doi.org/10.1042/bj3060071.

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Solubilization of opioid receptors from rat cortical membranes that retained high-affinity guanine nucleotide-sensitive agonist binding was achieved using 10 mM CHAPS. We report the nature of the interactions of mu and delta opioid receptors with the guanine nucleotide-binding protein G(o) by immunoprecipitation of CHAPS extracts with selective G(o)alpha-subunit protein antisera. Antiserum IM1 raised against amino acids 22-35 of G(o)alpha selectively co-immunoprecipitated G(o)alpha-mu and G(o)alpha-delta opioid receptor complexes detected in the immunoprecipitates by specific [3H][D-Ala2,N-Me-Phe4,Gly5-ol]enkephalin and [3H][D-Ser2,Leu5,Thr6]enkephalin binding respectively. By contrast, antisera directed against the C-terminal decapeptide (OC2) and the N-terminal hexadecapeptide (ON1) of isoforms of G(o)alpha were unable to immunoprecipitate solubilized opioid receptor-G(o) complexes, although both were able to immunoprecipitate solubilized G(o)alpha and have been shown to reduce the affinity of [D-Ala2,D-Leu5]enkephalin for opioid receptors in rat cortical membranes [Georgoussi, Carr and Milligan (1993) Mol. Pharmacol. 44, 62-69]. These findings demonstrate that CHAPS-solubilized mu and delta opioid receptors from rat cortical membranes form stable complexes with one or more variants of G(o).

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Kurzchalia, T. V., P. Dupree, R. G. Parton, R. Kellner, H. Virta, M. Lehnert, and K. Simons. "VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles." Journal of Cell Biology 118, no. 5 (September 1, 1992): 1003–14. http://dx.doi.org/10.1083/jcb.118.5.1003.

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In simple epithelial cells, apical and basolateral proteins are sorted into separate vesicular carriers before delivery to the appropriate plasma membrane domains. To dissect the putative sorting machinery, we have solubilized Golgi-derived transport vesicles with the detergent CHAPS and shown that an apical marker, influenza haemagglutinin (HA), formed a large complex together with several integral membrane proteins. Remarkably, a similar set of CHAPS-insoluble proteins was found after solubilization of a total cellular membrane fraction. This allowed the cloning of a cDNA encoding one protein of this complex, VIP21 (Vesicular Integral-membrane Protein of 21 kD). The transiently expressed protein appeared on the Golgi-apparatus, the plasma membrane and vesicular structures. We propose that VIP21 is a component of the molecular machinery of vesicular transport.

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33

Alrawi, Qutaiba K. J., Nada Nada, and S. Alzubydy. "Selection of Detergents Suitable for IBMR3 (Mab) using Balb/c Mouse Muscle." Cross Current International Journal of Medical and Biosciences 3, no. 8 (November 30, 2021): 75–82. http://dx.doi.org/10.36344/ccijmb.2021.v03i08.002.

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Monoclonal antibodies (Mab) and their fragments have been widely used for diagnostic and therapeutic purposes. Monoclonal antibodies IBMR3 hybridoma cells were produced in a previous study. In my study I used four types of detergents to fine the more suitable as the best Lysis buffer for monoclonal anti bodies using Balb/ c mouse tissue muscle. The four detergents includes; NP- 40, Igepal, Chaps and Triton X-100. Detergents were used in the laboratory to solubilize biological macromolecules such as proteins. These are none denaturing solvents; they also increase emulsification and solubilization, act as solubilize membrane proteins in their native state. The mouse samples were lysed in different lysis buffer detergents, the extracting protein where subjected on the SDS-PAGE electrophoresis, the separated protein bands were transferred to PVDF/ Polyvinylidene difluoride membrane for Immunoblotting technique. The immunblot were subsequently subjected to densitometry analysis to get the value of molecular weight, peak height and raw volume of the protein band. The results of muscle protein concentration of Blab/c mouse after using standard methods were shown (NP-40, 3.214 μg / μl), (Igepal, 3.647 μg / μl), (CHAPS, 3.925 μg / μl and Triton X-100, 4.214 μg / μl). The highest concentration of the muscle protein was obtained from using Triton X-100, followed by CHAPS, then by Igepal and in NP- 40.

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Coleman, R., K. Rahman, K. S. Kan, and R. A. Parslow. "Retrograde intrabiliary injection of amphipathic materials causes phospholipid secretion into bile. Taurocholate causes phosphatidylcholine secretion, 3-[(3-cholamidopropyl)dimethylammonio]-propane-1-sulphonate (CHAPS) causes mixed phospholipid secretion." Biochemical Journal 258, no. 1 (February 15, 1989): 17–22. http://dx.doi.org/10.1042/bj2580017.

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The control of biliary phospholipid and cholesterol secretions by bile acid was studied by using the technique of retrograde intrabiliary injection. Taurocholate (TC), a moderately hydrophobic bile acid, taurodehydrocholate (TDHC), a hydrophilic non-micelle-forming bile acid, and 3-[(3-cholamidopropyl)-dimethylammonio]propane-1-sulphonate (CHAPS), a detergent, were individually administered by retrograde intrabiliary injection (RII) into the biliary tree, and bile acids, phospholipids and cholesterol subsequently appearing in the bile were measured. TC (1.3 mumol; 45 microliters) injected retrogradely provoked a 3.5-fold increase in biliary phospholipid output for 40 min, as compared with the saline control. Injection of 2.7 mumol of TC (90 microliters) caused a 7.5-fold increase in phospholipid output, which reached a peak at 12 min after RII, and phospholipid output continued for 40 min. Cholesterol output was also elicited under these conditions, showing both dose-dependency and extended secretion. Injection of 1.8 mumol of TDHC caused very little increase in either biliary phospholipid or cholesterol. Injection of 0.9 mumol of CHAPS (45 microliters) provoked a single substantial peak of phospholipid output in the 3 min bile sample. T.l.c. analysis of the phospholipid extracts of the bile collected after each compound showed, for TC, a single compound which co-migrated with the phosphatidylcholine standard, whereas for CHAPS substantial amounts of other phospholipids were present.

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35

Bajo, Ana M., Juan C. Prieto, Pedro Valenzuela, Pilar Martinez, and Luis G. Guijarro. "Solubilization of Adenylyl Cyclase from Human Myometrium in a αS-Coupled Form." Bioscience Reports 23, no. 4 (August 1, 2003): 175–86. http://dx.doi.org/10.1023/b:bire.0000007691.17175.d9.

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Adenylyl cyclase (AC) was extracted from human myometrium with either non-ionic (Lubrol-PX or Triton X-100) or zwitterionic (3-[3-cholamidopropyl)dimethylammonio]-1-propanesulfonate, CHAPS) detergents. The soluble enzyme was stimulated by forskolin, a hydrophobic activator, in the presence of Mg2+ indicating that the catalytic subunit had not been damaged after solubilization. The enzyme was also activated by 5′-guanylyl imidodiphosphate (Gpp(NH)p) showing that the catalytic unit was not separated from stimulatory guanine nucleotide binding protein (Gs) during the extraction. Both activators showed different effects on the stimulatory efficacy and potency of AC activity solobulized with detergents. Gel filtration of Lubrol-PX and CHAPS extracts over a Sepharose CL-2B column partially resolved AC and its complexes. The chromatographic profile for Lubrolsolubilized AC presented a main peak of about 200 kDa whereas CHAPS-solubilized AC showed a dominant peak of about 1100 kDa. The heterodisperse peaks obtained revealed that the catalytic AC subunit was not separated from Gs proteins after gel filtration, and that AC could be associated with other cellular proteins. When Lubrol extract was submitted to anionic-exchange chromatography, the enzyme was purified about 7.5 fold (enzymatic activity of 48.1 pmol/min/mg of protein). The catalytic subunit was co-eluted with both AC-activating proteins Gαs large (52.2 kDa) and Gαs small (48.7 kDa). This is the first demonstration of the stable physical association of AC with both αs subunits of G proteins in human myometrium.

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Craxton, A., N. Ali, and S. B. Shears. "Comparison of the activities of a multiple inositol polyphosphate phosphatase obtained from several sources: a search for heterogeneity in this enzyme." Biochemical Journal 305, no. 2 (January 15, 1995): 491–98. http://dx.doi.org/10.1042/bj3050491.

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A multiple inositol polyphosphate phosphatase (formerly known as inositol 1,3,4,5-tetrakisphosphate 3-phosphatase) was purified approx. 22,000-fold from rat liver. The final preparation migrated on SDS/PAGE as a doublet with a mean apparent molecular mass of 47 kDa. Upon size-exclusion chromatography, the enzyme was eluted with an apparent molecular mass of 36 kDa. This enzyme was approximately evenly distributed between the ‘rough’ and ‘smooth’ subfractions of endoplasmic reticulum. There was a 20-fold range of specific activities of this phosphatase in CHAPS-solubilized particulate fractions prepared from the following rat tissues: liver, heart, kidney, testis and brain. However, each of these extracts contained different amounts of endogenous inhibitors of enzyme activity. After removal of these inhibitors by MonoQ anion-exchange chromatography, there was only a 2.5-fold range of specific activities; kidney contained the most and brain contained the least. We prepared and characterized polyclonal antiserum to the hepatic phosphatase, which immunoprecipitated 85-100% of both particulate and soluble phosphatase activities. The antiserum also immunoprecipitated, with equivalent efficacy, CHAPS-solubilized phosphatase activities from heart, kidney, testis, brain and erythrocytes (all prepared from rat). Our data strengthen the case that the function of the mammalian phosphatase is unrelated to the metabolism of Ca(2+)-mobilizing cellular signals. The CHAPS-solubilized phosphatase from turkey erythrocytes was not immunoprecipitated by the polyclonal antiserum, and is therefore an isoform that is structurally distinct, and possibly functionally unique.

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Filenko, Nina A., Dmytro B. Palets, and Yuri L. Lyubchenko. "Structure and Dynamics of Dinucleosomes Assessed by Atomic Force Microscopy." Journal of Amino Acids 2012 (October 23, 2012): 1–6. http://dx.doi.org/10.1155/2012/650840.

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Dynamics of nucleosomes and their interactions are important for understanding the mechanism of chromatin assembly. Internucleosomal interaction is required for the formation of higher-order chromatin structures. Although H1 histone is critically involved in the process of chromatin assembly, direct internucleosomal interactions contribute to this process as well. To characterize the interactions of nucleosomes within the nucleosome array, we designed a dinucleosome and performed direct AFM imaging. The analysis of the AFM data showed dinucleosomes are very dynamic systems, enabling the nucleosomes to move in a broad range along the DNA template. Di-nucleosomes in close proximity were observed, but their population was low. The use of the zwitterionic detergent, CHAPS, increased the dynamic range of the di-nucleosome, facilitating the formation of tight di-nucleosomes. The role of CHAPS and similar natural products in chromatin structure and dynamics is also discussed.

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Sobel, David. "Sumner on Welfare." Dialogue 37, no. 3 (1998): 571–77. http://dx.doi.org/10.1017/s0012217300020503.

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L. W. Sumner's excellent book Welfare, Happiness, and Ethics has four central goals. He aims (1) to demonstrate the subjectivity of welfare (chaps. 1 to 3); (2) to show that the traditional subjective accounts of welfare—namely, hedonism and preference theories—are inadequate (chaps. 4 and 5); (3) to construct an alternative subjectivist account of welfare (chapter 6); and (4) to argue for the moral primacy of welfare (chap. 7). I will not comment here on Sumner's treatment of the subjectivity of welfare, as I have had my say on this topic elsewhere. In fact, my space here will only permit me to discuss the second and fourth goals of the book. Even with this narrow focus, I will be forced to leave unexplored a wealth of truly lovely work which passes by us on the road to these central conclusions.

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Hall, Scott W., and Scott R. VandenBerg. "Solid Phase Extraction of the Zwitterionic Detergent Chaps." Preparative Biochemistry 19, no. 1 (January 1989): 1–11. http://dx.doi.org/10.1080/10826068908544892.

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Kulkarni, A., S. Shetty, and F. Damda. "G443(P) "CHAPS" handover tool in Paediatric setting." Archives of Disease in Childhood 99, Suppl 1 (April 1, 2014): A185. http://dx.doi.org/10.1136/archdischild-2014-306237.425.

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Lazar, Nicole A., and David S. Sidore. "Math Chaps and other Oddities: Statisticians in Literature." CHANCE 16, no. 2 (March 2003): 33–37. http://dx.doi.org/10.1080/09332480.2003.10554846.

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42

Merchán, M. D., and M. M. Velázquez. "Properties of CHAPS micelles modulated by different polyelectrolytes." Colloids and Surfaces A: Physicochemical and Engineering Aspects 366, no. 1-3 (August 2010): 12–17. http://dx.doi.org/10.1016/j.colsurfa.2010.05.009.

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43

Basu, Abhijit, Rohit Arora, and Nancy Fernandes. "Onsite handover of clinical care: implementing modified CHAPS." Clinical Governance: An International Journal 16, no. 3 (August 9, 2011): 220–30. http://dx.doi.org/10.1108/14777271111153813.

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Sivaprasadarao, A., M. Boudjelal, and J. B. C. Findlay. "Solubilization and purification of the retinol-binding protein receptor from human placental membranes." Biochemical Journal 302, no. 1 (August 15, 1994): 245–51. http://dx.doi.org/10.1042/bj3020245.

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The membrane receptor for retinol-binding protein (RBP) has been solubilized from human placental brush-border membranes with octyl-beta-glucoside, Nonidet P-40 and CHAPS. A method, based on the preferential precipitation of 125I-RBP-receptor complex with poly(ethylene glycol) 8000, was developed in order to measure the RBP-binding activity in the detergent extracts. The receptor was fairly stable (4 degrees C, 7 days) in octyl-beta-glucoside and Nonidet P-40, but quickly lost activity in CHAPS. The detergent-solubilized form retained all the properties characteristic of the membrane-bound protein, except for a small decrease in affinity for RBP (3- and 7-fold in Nonidet P-40 and octyl-beta-glucoside respectively). The receptor was isolated using recombinant RBP coupled to Reacti-Gel 6X affinity matrix. The purified material contained major and minor protein species of 63 and 55 kDa respectively on SDS/PAGE.

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Xiao, Z., and P. N. Devreotes. "Identification of detergent-resistant plasma membrane microdomains in dictyostelium: enrichment of signal transduction proteins." Molecular Biology of the Cell 8, no. 5 (May 1997): 855–69. http://dx.doi.org/10.1091/mbc.8.5.855.

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Unlike most other cellular proteins, the chemoattractant receptor, cAR1, of Dictyostelium is resistant to extraction by the zwitterionic detergent, CHAPS. We exploited this property to isolate a subcellular fraction highly enriched in cAR1 by flotation of CHAPS lysates of cells in sucrose density gradients. Immunogold electron microscopy studies revealed a homogeneous preparation of membrane bilayer sheets. This preparation, designated CHAPS-insoluble floating fraction (CHIEF), also contained a defined set of 20 other proteins and a single uncharged lipid. Cell surface biotinylation and preembedding immunoelectron microscopy both confirmed the plasma membrane origin of this preparation. The cell surface phosphodiesterase (PDE) and a downstream effector of cAR1, adenylate cyclase (ACA), were specifically localized in these structures, whereas the cell adhesion molecule gp80, most of the major cell surface membrane proteins, cytoskeletal components, the actin-binding integral membrane protein ponticulin, and G-protein alpha- and beta-subunits were absent. Overall, CHIFF represents about 3-5% of cell externally exposed membrane proteins. All of these results indicate that CHIFF is derived from specialized microdomains of the plasma membrane. The method of isolation is analogous to that of caveolae. However, we were unable to detect distinct caveolae-like structures on the cell surface associated with cAR1, which showed a diffuse staining profile. The discovery of CHIFF facilitates the purification of cAR1 and related signaling proteins and the biochemical characterization of receptor-mediated processes such as G-protein activation and desensitization. It also has important implications for the "fluid mosaic" model of the plasma membrane structures.

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46

Luan, Zhiqiang, Wenshuai Liu, Yu Xia, Ruochong Zhang, Bohua Feng, Xiaodong Hu, Shuiquan Huang, and Xuefeng Xu. "Effects of an Electrical Double Layer and Tribo-Induced Electric Field on the Penetration and Lubrication of Water-Based Lubricants." Lubricants 10, no. 6 (June 2, 2022): 111. http://dx.doi.org/10.3390/lubricants10060111.

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Understanding the effects of electrical double layers (EDL) and tribo-induced electric fields on the electroosmotic behaviors of lubricants is important for developing high-performance water-based lubricants. In this study, EDL conductivities of aqueous lubricants containing a surfactant of 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate (CHAPS) or cetyltrimethylammonium bromide (CTAB) were analyzed. The interfacial zeta potentials of the synthesized lubricants and Al2O3 ceramic-alloy steel contacts were measured, and frictional potentials of ceramic and steel surfaces were determined using a modified ball-on-disc configuration. The distribution characteristics of the tribo-induced electric field of the ceramic-steel sliding contact were numerically analyzed. The electroosmotic behaviors of the lubricants were investigated using a four-ball configuration. It was found that an EDL and tribo-induced electric field was a crucial enabler in stimulating the electroosmosis of lubricants. Through altering EDL structures, CHAPS enhanced the electroosmosis and penetration of the water-based lubricant, thus resulting in improved lubrication.

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Willis, John T. "National “Beauty” and Yahweh’s “Glory” as a Dialectical Key to Ezekielian Theology." Horizons in Biblical Theology 34, no. 1 (2012): 1–18. http://dx.doi.org/10.1163/187122012x602567.

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Abstract The message of the book of Ezekiel is addressed to three nations: Phoenicia (chaps 26-28), Egypt (chaps 29-32), and Judah. Its judgment oracles are predominantly “announcements of doom.” But at certain junctures the author states the “reason” for the coming destruction. In each case, the fundamental “reason” for imminent divine punishment is trust in one’s own “beauty” (yph): Phoenicia (27:3, 4, 11; 28:12, 17); Egypt (31:3, 8, 9); Judah (16:14, 15, 25). In stark contrast to this self-fascination, Yahweh’s “glory” (kbd) appears in a theophanic vision recurring throughout the book: over against Phoenicia (18:22), Egypt (31:18, by implication), and Judah/Jerusalem (1:28; 3:12, 23 [2x]; 8:4; 9:3; 10:4 [2x], 18, 19; 11:22, 23; 43:2 [2x], 4, 5; 44:4). This dialectic between Yahweh’s “glory” and nations’ preoccupation with their own “beauty” seems to be the theological thread which holds the book of Ezekiel together.

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Harvey, H. J., M. A. Venis, and A. J. Trewavas. "Partial purification of a protein from maize (Zea mays) coleoptile membranes binding the Ca2+-channel antagonist verapamil." Biochemical Journal 257, no. 1 (January 1, 1989): 95–100. http://dx.doi.org/10.1042/bj2570095.

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A protein that binds the calcium-channel antagonist verapamil has been partially purified from maize (Zea mays) coleoptile membranes. The protein was solubilized with the detergent CHAPS ([ 3-(3-cholamidopropyl)dimethylammonio]propane-1-sulphonate) and purified by a combination of ion-exchange, gel-filtration and hydrophobic-interaction chromatography. This resulted in a 120-fold purification. SDS/polyacrylamide-gel-electrophoretic analysis of the polypeptides from the final purification step indicated that the verapamil-binding protein may have a major component of Mr 169,000. The dissociation constants for specific binding of [3H]verapamil to crude and CHAPS-solubilized maize coleoptile membrane fractions are 72 nM and 158 nM respectively, with respective binding-site concentrations of 135 pmol/mg of protein and 78 pmol/mg of protein. In both cases the Scatchard plots are linear, indicating a single class of binding sites. [3H]Verapamil binding to crude maize coleoptile membrane fractions could not be displaced by unlabelled desmethoxyverapamil or by nifedipine, but could be displaced by unlabelled methoxyverapamil.

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49

Centlow, Magnus, Stefan R. Hansson, and Charlotte Welinder. "Differential Proteome Analysis of the Preeclamptic Placenta Using Optimized Protein Extraction." Journal of Biomedicine and Biotechnology 2010 (2010): 1–9. http://dx.doi.org/10.1155/2010/458748.

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The human placenta is a difficult tissue to work with using proteomic technology since it contains large amounts of lipids and glycogen. Both lipids and glycogen are known to interfere with the first step in the two-dimensional polyacrylamide gel electrophoresis (2D-PAGE), the isoelectric focusing. In order to gain the best possible protein separation on 2D-PAGE, an optimized sample preparation protocol for placental proteins was developed. Two different buffers, urea/CHAPS and Hepes, were used for solubilization in combination with six different precipitation methods. The removal of glycogen from the samples by centrifugation was crucial for the final proteome maps. Solubilization with urea/CHAPS in combination with dichloromethane/methanol or acidified acetone proved to be the best precipitation procedures. When applied to clinical placenta samples apolipoprotein A1 was found to be accumulated in the preeclamptic placenta, where it may either have a nutritional effect or act as a modifier of signal transduction.

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Pineda Guerra, Yessica, Johana Betancur Echeverri, Johanna Pedroza-Díaz, Edilson Delgado-Trejos, and Sarah Röthlisberger. "Análisis proteómico del veneno de la abeja africanizada: comparación de métodos de extracción." Acta Biológica Colombiana 21, no. 3 (August 30, 2016): 619. http://dx.doi.org/10.15446/abc.v21n3.54046.

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La abeja africanizada es la más común en la apicultura colombiana y a su veneno (apitoxina) se le han atribuido propiedades terapéuticas para diferentes enfermedades, sin mayor soporte científico. Al revisar en la literatura los reportes publicados sobre el análisis proteómico de la apitoxina, se encontraron cuatro métodos distintos para la extracción de proteínas de la apitoxina. El primer método consiste en resuspender la apitoxina en Urea 7 M, precipitar con acetona y finalmente resuspender en Urea 7 M y CHAPS 4 %. Para el segundo método se resuspende la apitoxina en buffer de lisis, se precipita con ácido tricloroacético, y luego se resuspende en Urea 7 M y CHAPS 4 %. El tercer método es igual al anterior, excepto que la precipitación se realiza con acetona en vez de ácido tricloroacético. Finalmente, el cuarto método consiste en resuspender la apitoxina en agua destilada, precipitar con acetona y resuspender en Urea 7 M y CHAPS 4 %. Este trabajo se enfocó en comparar el desempeño de estos cuatro métodos de extracción y determinar el método con el mejor resultado en cuanto a la concentración e integridad obtenida de las proteínas. De los distintos métodos evaluados, se encontró que los mejores resultados en cuanto a concentración de proteínas se obtuvieron con la resuspensión de apitoxina en buffer de lisis y precipitación con acetona (método 3) y con el método de resuspensión de apitoxina en agua destilada y precipitación con acetona (método 4). De estos, el mejor método de extracción en cuanto a integridad de las proteínas y perfil proteómico fue el de resuspensión de apitoxina en buffer de lisis seguido de precipitación con acetona (método 3).

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Journal articles on the topic 'CHAPS'

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