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Статті в журналах з теми "Sodium phosphate buffer"
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Ali, Maysaa Adil. "Optimizing Extraction Conditions of Actinidin from Kiwifruit (Actinidia deliciosa)." Al-Mustansiriyah Journal of Science 28, no. 3 (July 3, 2018): 61. http://dx.doi.org/10.23851/mjs.v28i3.57.
Повний текст джерелаАнотація:
Kiwifruit (Actinidia deliciosa) is one many fruits that is rich of enzymes like Actinidin. Actinidin is a member of cysteine protease. In this study, different parameters and conditions were tested for optimal Actinidin extraction from kiwifruit. The tested parameters are optimum buffers, pH, Molarity, time, and amounts (gm) of kiwifruit to volume (ml) of buffer ratio. The best buffer for Actinidin extraction from kiwifruit was Sodium phosphate because it gave high activity, with casein as a substrate. The next experiments used sodium phosphate as an optimal buffer for Actinidin extraction and casein as a substrate, detected the optimal Actinidin extraction conditions were carried out at pH 7.0, 0.1 M of sodium phosphate, 2.5 min of extraction time, 1:0.5 (gm of kiwifruit fruit/ v of sodium phosphate buffer) extraction percentage, and 30 min of incubation time. Also this study showed that the maximum enzyme activity for Actinidin extracted from kiwifruit was at pH 7and at 30 min of incubation with casein as substrate.
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Kim, Soo Hyun, Han Ju Yoo, Eun Ji Park, and Dong Hee Na. "Nano Differential Scanning Fluorimetry-Based Thermal Stability Screening and Optimal Buffer Selection for Immunoglobulin G." Pharmaceuticals 15, no. 1 (December 25, 2021): 29. http://dx.doi.org/10.3390/ph15010029.
Повний текст джерелаАнотація:
Nano differential scanning fluorimetry (nanoDSF) is a high-throughput protein stability screening technique that simultaneously monitors protein unfolding and aggregation properties. The thermal stability of immunoglobulin G (IgG) was investigated in three different buffers (sodium acetate, sodium citrate, and sodium phosphate) ranging from pH 4 to 8. In all three buffers, the midpoint temperature of thermal unfolding (Tm) showed a tendency to increase as the pH increased, but the aggregation propensity was different depending on the buffer species. The best stability against aggregation was obtained in the sodium acetate buffers below pH 4.6. On the other hand, IgG in the sodium citrate buffer had higher aggregation and viscosity than in the sodium acetate buffer at the same pH. Difference of aggregation between acetate and citrate buffers at the same pH could be explained by a protein–protein interaction study, performed with dynamic light scattering, which suggested that intermolecular interaction is attractive in citrate buffer but repulsive in acetate buffer. In conclusion, this study indicates that the sodium acetate buffer at pH 4.6 is suitable for IgG formulation, and the nanoDSF method is a powerful tool for thermal stability screening and optimal buffer selection in antibody formulations.
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Yuan, Zhiguo, Shanshan Duan, Jingsong Shen, and Youzhi Liu. "Sulfur Capacity of Sodium Phosphate Buffer Solution." JOURNAL OF CHEMICAL ENGINEERING OF JAPAN 52, no. 2 (February 20, 2019): 204–9. http://dx.doi.org/10.1252/jcej.18we018.
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Yu, A. W., C. B. Leung, P. K. T. Li, S. F. Lui, and K. N. Lai. "Pain Perception following Subcutaneous Injections of Citrate-Buffered and Phosphate-Buffered Epoetin Alpha." International Journal of Artificial Organs 21, no. 6 (June 1998): 341–43. http://dx.doi.org/10.1177/039139889802100612.
Повний текст джерелаАнотація:
Subcutaneous injection of citrate-buffered epoetin alpha (EPO-α) causes pain. Substitution of citrate buffer with a phosphate buffer in the EPO-α resulted in a significant reduction in duration and severity of pain. It is possible that sodium citrate which is present in the EPO-α may be the agent that causes discomfort in the patients.
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Suurkuusk, Malin, and Dan Hallén. "Investigation of guanidine hydrochloride induced unfolding of apolipoprotein A-IMilano." Spectroscopy 16, no. 3-4 (2002): 199–206. http://dx.doi.org/10.1155/2002/201073.
Повний текст джерелаАнотація:
A guanidine hydrochloride (GuHCl) induced unfolding study of apolipoprotein A-IMilano(apo A-IM) has been performed. The unfolding was followed by circular dichroism (CD) measurements at 222 nm and by isothermal titration (ITC) calorimetry at 25°C. In the ITC experiments enthalpies of transfer were determined for apo A-IMfrom aqueous sodium phosphate buffer solution into solutions of different concentrations of GuHCl. The CD data and the ITC data give complementary and consistent results of the complex unfolding process. Analytical ultracentrifugation experiments were made on apo A-IMin sodium phosphate buffer and in 0.6 M GuHCl, respectively. Analyses of the obtained sedimentation velocity data show that apo A-IMis highly aggregated in sodium phosphate buffer. The aggregates are almost completely dissociated in 0.6 M GuHCl. Aggregation of the protein in sodium phosphate buffer solution induces an increase in α-helical content. The loss of α-helical secondary structural element of the protein upon dissociation of the aggregates destabilises the protein resulting in a low GuHCl concentration of unfolding, [GuHCl]m=1.1 M. The unfolded protein has a significant α-helical content at the unfolded state. From ITC- and CD data we suggest that increased binding of GuHCl to the unfolded protein results in a disruption of the residual secondary structure.
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Spitsberg, Vitaly L., Liza Ivanov, and Vladimir Shritz. "Recovery of milk fat globule membrane (MFGM) from buttermilk: effect of Ca-binding salts." Journal of Dairy Research 86, no. 3 (August 2019): 374–76. http://dx.doi.org/10.1017/s002202991900061x.
Повний текст джерелаАнотація:
AbstractIn this Research Communication we present a study of the effect of Ca-binding salts on the recovery of milk fat globule membrane (MFGM) from buttermilk. Sodium phosphate buffer was used for the purpose of MFGM recovery from buttermilk for the first time and we showed that 0.1 M buffer at pH 7.2 was the most effective for the recovery of MFGM. The fact of high efficacy of sodium phosphate buffer in recovery of MFGM from buttermilk allowed us to suggest that MFGM in buttermilk is present in association with casein through Ca- bridges formed between phospholipids of MFGM and phosphate groups of casein, primarily with k-casein as the peripheral protein of casein micelles.
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Okada, Toshihiko, Minoru Miyakoshi, Masao Inoue, Mayumi Miyanabe, Yasuko Ueno, and Yasuko Nakabayashi. "Differential elution from a Sephadex G-15 column of sodium and phosphate ions of sodium phosphate with sodium or potassium phosphate buffer." Journal of Chromatography A 604, no. 2 (July 1992): 219–24. http://dx.doi.org/10.1016/0021-9673(92)85131-c.
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Olmos, J. M., M. A. Lasunción, and E. Herrera. "Dextran Sulfate Complexes with Potassium Phosphate to Interfere in Determinations of High-Density Lipoprotein Cholesterol." Clinical Chemistry 38, no. 2 (February 1, 1992): 233–37. http://dx.doi.org/10.1093/clinchem/38.2.233.
Повний текст джерелаАнотація:
Abstract The interference of dextran sulfate with the colorimetric determination of free cholesterol causes an increase in the absorbance that is proportional to the dextran sulfate concentration in the sample. This makes estimation of the free cholesterol concentration unreliable in high-density lipoprotein-containing supernates obtained after plasma precipitation with dextran sulfate/MgCl2. Analysis of the absorption spectrum demonstrated that the absorbance increase was due to turbidity. We observed this effect with colorimetric reagents based on potassium phosphate buffer but not with those based on sodium phosphate or Tris buffers. This effect is ascribed to dextran sulfate because neither the omission of Mg2+ ions nor their chelation with EDTA prevented turbidity, whereas precipitation of dextran sulfate with Ba2+ counteracted this effect. Therefore, potassium phosphate-buffered reagents appear unsuitable for colorimetric lipid determinations in samples containing dextran sulfate.
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Pinta Rizki Mala Hasibuan, Mitha Alviyulita, and Farida Hanum. "PENGARUH PENAMBAHAN NATRIUM KLORIDA (NaCl) DAN WAKTU PERENDAMAN BUFFER FOSFAT TERHADAP PEROLEHAN CRUDE PAPAIN DARI DAUN PEPAYA (CARICA PAPAYA, L.)." Jurnal Teknik Kimia USU 3, no. 3 (September 30, 2014): 39–44. http://dx.doi.org/10.32734/jtk.v3i3.1642.
Повний текст джерелаАнотація:
Papaya (Carica papaya L.) is one of the fruits of commodities internationally, either in the form of fresh fruit or as processed products. The leaves are green still not fully utilized. Papaya leaves contains papain enzyme which is a protease enzyme that very helpful for the industry. Papain is a protease enzyme contained in papaya latex, whether in fruit, stems and leaves, as an enzyme capable of solving the protein molecules, current papain into products that are beneficial to human life, either at home or industrial ladder. This study aims to determine the effect of the degree of saturation of sodium chloride and phosphate buffer to yield soaking rough papaya protease. This study varying the time of immersion phosphate buffer and saturation levels of sodium chloride. Analysis of protease activity was performed using UV-Vis spectrophotometer to measure the wavelength and absorbance values. The best research results obtained at 12 h immersion phosphate buffer with a concentration of sodium chloride 60% is 272.8222 unit / ml. In the analysis of the rendemen obtained by the best condition at the time of immersion phosphate buffer for 36 hours at a concentration of 90% is 43,5152%. In the analysis of moisture content obtained the best condition at the time of immersion of 36 hours at a concentration of 90% is 37.4266%.
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Sokołowska, Magdalena, Krystyna Pawlas, and Wojciech Bal. "Effect of Common Buffers and Heterocyclic Ligands on the Binding of Cu(II) at the Multimetal Binding Site in Human Serum Albumin." Bioinorganic Chemistry and Applications 2010 (2010): 1–7. http://dx.doi.org/10.1155/2010/725153.
Повний текст джерелаАнотація:
Visible-range circular dichroism titrations were used to study Cu(II) binding properties of Multimetal Binding Site (MBS) of Human Serum Albumin (HSA). The formation of ternary MBS-Cu(II)-Buffer complexes at pH 7.4 was positively verified for sodium phosphate, Tris, and Hepes, the three most common biochemical buffers. The phosphate > Hepes > Tris order of affinities, together with strong spectral changes induced specifically by Tris, indicates the presence of both Buffer-Cu(II) and Buffer-HSA interactions. All complexes are strong enough to yield a nearly 100% ternary complex formation in 0.5 mM HSA dissolved in 100 mM solutions of respective buffers. The effects of warfarin and ibuprofen, specific ligands of hydrophobic pockets I and II in HSA on the Cu(II) binding to MBS were also investigated. The effects of ibuprofen were negligible, but warfarin diminished the MBS affinity for Cu(II) by a factor of 20, as a result of indirect conformational effects. These results indicate that metal binding properties of MBS can be modulated directly and indirectly by small molecules.
Дисертації з теми "Sodium phosphate buffer"
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COSSU, ANTONELLA. "Introduzione alla veicolazione transdermica dell’Ibuprofene Sale Sodico e quantificazione in HPLC." Doctoral thesis, Università degli Studi di Cagliari, 2014. http://hdl.handle.net/11584/266438.
Повний текст джерелаАнотація:
The aim of this work is to quantify the Ibuprofen sodium salt in samples derived from Franz cells transdermal delivery experiments.
An analytical method for a determination of Ibuprofen sodium salt and Diclofenac sodium salt (used as internal standard) has been developed, assuring rapidity, accuracy, precision, selectivity and a minimal treatment of the sample.
With this method we have been able to analized not only the sample obtained from the recipient cell, but also the skin and the formulation used in the experiment.
To this aim a methods that would allow the easy removal of the drug from the tissue has been developped.
In this way, it was easy to verify the real quantification of the drug in all phases of the experiment and quantify its total delivery.
In order to perform High Performance Liquid Cromatography (HPLC) analysis, human skin used in experiment has been dissolved first and then deproteinized.
The effectiveness of deproteinization performed through methods such as precipitation with organic solvent, cryo-treatment, Amicon filter tubes, HybridSpe cartridges and Folch method has been verified through the use of the NanoOrange kit.
For the HPLC method, the working conditions were as follows: RP18 column EC 150/4,6 NUCLEODUR® 100-5 C18 ec, Macherey-Nagel GmbH & Co. KG protected with a guard column (EC 4/3 NUCLEODUR®, 100-5 C18 ec, 100-5 18 ec, Macherey-Nagel GmbH & Co. KG) and a pre-column (cut-off: 0,2 μm, Supelco, n. cat. 55215-U); mobile phase phosphate buffer 25 mM - Acetonitrile (73:27 v/v) (pH 7) adjusted with hydrochloric acid; flow 1.0 mL/min.; injection volume of 20 μL; and UV detection was carried out at 265 nm, and experiment were performed in a room where temperature was constantly kept at 25°C.
With this method, the detection of a drug concentration in a range between 0.03 - 7.69 μg/mL has been allowed.
Therefore, the proposed method can be successfully used for drug analysis in samples derived from transdermal delivery experiments.
2
Gómez, Gerardo. "Crystallization-related pH changes during freezing of sodium phosphate buffer solutions." 1995. http://catalog.hathitrust.org/api/volumes/oclc/68798121.html.
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Ou, Shih-fu, and 歐士輔. "Phase Transformation Study of MCPM Added CaCO3 and Mixed with Sodium Phosphate Buffer Solution in Different pH Value." Thesis, 2005. http://ndltd.ncl.edu.tw/handle/56220138096576694753.
Повний текст джерелаАнотація:
碩士國立臺灣科技大學
機械工程系
93
In order to develop filling material of calcium phosphate cement(CPC) applied to dentistry or orthopaedy, a CPC was prepared by mixing monocalcium phosphate monohydrate(MCPM), calcium carbonate (CaCO3) and sodium phosphate buffer solution with an overall Ca/P mole ratio 1.33 at 37℃. To understand the effect of pH value on formation of CPC, several sodium phosphate buffer solution were prepared at pH4.1, pH5.1, pH6.0, pH7.0, pH8.0 and pH9.1, respectively. The synthetic CPC were analyzed by x.ray diffraction (XRD) method and fourier transform infrared (FTIR) to determined the phase component of products. The physical properties were estimated by measured setting time and compressive strength. The morphology of CPC crystal was observed using scanning electron microscopy (SEM), and the microstructure was investigated by transmitted electron microscopy (TEM). The results show that the products of CPC in different pH phosphate buffer solution are the mixtures consist of Ca-deficient hydroxyapatite (CDHA), dicalcium phosphate dihydrate (CaHPO4•2H2O; DCPD) and dicalcium phosphate anhydrate (CaHPO4; DCPA). With increasing pH value of additional source of phosphate buffer solution, the CPC cements obtain more quantities of CDHA. Meanwhile, they harden in relatively short time and obtain higher compressive strength. The phase evolution with aging is in three steps. First, monocalcium phosphate monohydrate (Ca(H2PO4)2•H2O; MCPM), and carbonate calcium (CaCO3) crystal are dissolved in sodium phosphate buffer solution and precipitate DCPD crystal. Secondly, after about 12 hours, a conversion of DCPD to intermediate amorphous calcium phosphate (ACP) is begun, on the other hand, remained DCPD would be converted into DCPA. Finally, the metastable ACP phase would be converted into stable CDHA.
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VOTTARIELLO, FRANCESCA. "OLIGOMERIZATION OF RNase A:a) A STUDY OF THE INFLUENCE OF SERINE 80 RESIDUE ON THE 3D DOMAIN SWAPPING MECHANISMb) “ZERO-LENGTH” DIMERS OF RNase A AND THEIR CATIONIZATION WITH PEI." Doctoral thesis, 2010. http://hdl.handle.net/11562/344075.
Повний текст джерелаАнотація:
"Zero-length" dimers of ribonuclease A, a novel type of dimers formed by two RNase A molecules bound to each other through a zero-length amide bond [Simons, B.L. et al. (2007) Proteins 66, 183-195], were analyzed, and tested for their possible in vitro cytotoxic activity. Results: (i) Besides dimers, also trimers and higher oligomers can be identified among the products of the covalently linking reaction. (ii) The "zero-length" dimers prepared by us appear not to be a unique species, as was instead reported by Simons et al. The product is heterogeneous, as shown by the involvement in the amide bond of amino and carboxyl groups others than only those belonging to Lys66 and Glu9. This is demonstrated by results obtained with two RNase A mutants, E9A and K66A. (iii) The "zero-length" dimers degrade poly(A).poly(U) (dsRNA) and yeast RNA (ssRNA): while the activity against poly(A).poly(U) increases with the increase of the oligomer's basicity, the activity towards yeast RNA decreases with the increase of oligomers' basicity, in agreement with many previous data, but in contrast with the results reported by Simons et al. (iv) No cytotoxicity against various tumor cells lines could be evidenced in RNase A "zero-length" dimers. (v) They instead become cytotoxic if cationized by conjugation with polyethylenimine [Futami, J. et al. (2005) J. Biosci. Bioengin. 99, 95-103]. However, polyethylenimine derivatives of RNase A "zero-length" dimers and native, monomeric RNase A are equally cytotoxic. In other words, protein "dimericity" does not play any role in this case. Moreover, (vi) cytotoxicity seems not to be specific for tumor cells: polyethylenimine-cationized native RNase A is also cytotoxic towards human monocytes."Zero-length" dimers of ribonuclease A, a novel type of dimers formed by two RNase A molecules bound to each other through a zero-length amide bond [Simons, B.L. et al. (2007) Proteins 66, 183-195], were analyzed, and tested for their possible in vitro cytotoxic activity. Results: (i) Besides dimers, also trimers and higher oligomers can be identified among the products of the covalently linking reaction. (ii) The "zero-length" dimers prepared by us appear not to be a unique species, as was instead reported by Simons et al. The product is heterogeneous, as shown by the involvement in the amide bond of amino and carboxyl groups others than only those belonging to Lys66 and Glu9. This is demonstrated by results obtained with two RNase A mutants, E9A and K66A. (iii) The "zero-length" dimers degrade poly(A).poly(U) (dsRNA) and yeast RNA (ssRNA): while the activity against poly(A).poly(U) increases with the increase of the oligomer's basicity, the activity towards yeast RNA decreases with the increase of oligomers' basicity, in agreement with many previous data, but in contrast with the results reported by Simons et al. (iv) No cytotoxicity against various tumor cells lines could be evidenced in RNase A "zero-length" dimers. (v) They instead become cytotoxic if cationized by conjugation with polyethylenimine [Futami, J. et al. (2005) J. Biosci. Bioengin. 99, 95-103]. However, polyethylenimine derivatives of RNase A "zero-length" dimers and native, monomeric RNase A are equally cytotoxic. In other words, protein "dimericity" does not play any role in this case. Moreover, (vi) cytotoxicity seems not to be specific for tumor cells: polyethylenimine-cationized native RNase A is also cytotoxic towards human monocytes.
Тези доповідей конференцій з теми "Sodium phosphate buffer"
1
Park, Jong Woon, Byung Gi Park, and Chang Hyun Kim. "Investigation of Chemical Effects on Emergency Core Cooling Filtration Head Loss After Loss of Coolant Accident." In 17th International Conference on Nuclear Engineering. ASMEDC, 2009. http://dx.doi.org/10.1115/icone17-75398.
Повний текст джерелаАнотація:
Integrated tests of head loss through an emergency core cooling filter screen are conducted, simulating reactor building environmental conditions for thirty days after a loss of coolant accident. A test apparatus with five individual loops each of whose chamber is established to test chemical product formation and measure the head loss through a sample filter. The screen area at each chamber is 78.54cm2 and reactor building materials can be scaled down according to specific plant condition. A series of tests have been performed to investigate the effects of reactor building spray, existence of calcium-silicate with tri-sodium phosphate (TSP), and composition of materials. The results showed that head loss across the chemical bed with even a small amount of calcium-silicate insulation instantaneously increased as soon as TSP was added to the test solution. Also, the head loss across the filter screen is strongly affected by spray duration and the head loss increase is rapid at the early stage, because of high dissolution and precipitation of aluminum and zinc. After passivation of aluminum and zinc by corrosion, the head loss increase is much slowed down and is mainly induced by materials such as calcium, silicon, and magnesium leached from NUKON™ and concrete. Furthermore, it is newly found that the spay buffer agent, tri-sodium phosphate, to form protective coating on the aluminum surface and reduce aluminum leaching is not effective for a large amount of aluminum and a long spray.
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PEERSCHKE, E. IB, and B. Ghebrehiwet. "CHARACTERIZATION OF HUMAN PLATELET ClQ BINDING SITES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643503.
Повний текст джерелаАнотація:
We have recently shown that platelets possess specific binding sites for Clq, a subcomponent of the first component of complement, Cl, and that occupancy of these receptor sites correlates with the previously described inhibitory effect of Clq on collagen-induced platelet aggregation. To further characterize platelet Clq receptors, washed platelets were solubilized in 5 mM sodium phosphate buffer, pH 7.5 containing 10 mM EDTA, 150 mM NaCl, 10 mM EACA, 0.5 mM PMSF, and 1% Triton X-100. After dialysis against 5 mM phosphate buffer pH 7.5 containing 10 mM EDTA, 20 mM NaCl, 10 mM EACA,0.5 mM PMSF and 0.1% Triton X-100, the lysate was passed over Clq-Sepharose-4B affinity columns. A single protein peak eluted with buffer containing 300 mM NaCl. This peak was composed of two predominant molecular weight species (85-95K, 60-66K) as assessed by SDS-polyacrylamide gel electrophoresis under non-reducing conditions. When 125-iodine surface labeled platelets were solubilized and applied to Clq-Sepharose affinity resins, the same two molecular weight species eluted and could be visualized by autoradiography following SDS-polyacrylamide gel electrophoresis. Immunoabsorption studies performed under nondenaturing conditions using protein A and the IIl/Dl monoclonal antibody, which binds specifically to platelets and inhibits platelet-Clq interactions, revealed that the 85-95K molecular weight component was preferentially absorbed, but incomplete immunoabsorption of the 60-66K molecular weight constituent was also noted. Affinity purified Clq binding sites sedimented as a single peak during 5-40% sucrose density ultracentrifugation with an S value of approximately 2.4. In addition, both the 85-95K and the 60-66K molecular weight species coeluted in the void volume of Sephadex G-100 columns. The data suggest that the 85-95K and 60-66K molecular weight species represent platelet membrane Clq binding sites, and that these sites may form weak, noncovalently associated complexes.
3
Chang, Tsung-Yao, and Chii-Wann Lin. "Solutions of SAT Problems Solved by a SPR-Based DNA Processor." In ASME 2008 First International Conference on Micro/Nanoscale Heat Transfer. ASMEDC, 2008. http://dx.doi.org/10.1115/mnht2008-52036.
Повний текст джерелаАнотація:
DNA computation has shown its potential not only on mathematics, but on various practical areas such as diagnosis, single nucleotide polymorphism (SNP) detection, smart amplification, encryption and drug delivery etc. However, most previous researches about DNA computation possess a couple of weaknesses, including time-wasting, effort-wasting, lack of reusability and no miniaturization. In order to address this issue and improve weaknesses mentioned above, we built up a surface plasmon resonance (SPR) system for the detection on the DNA array chip to solve a 3-clause satisfiability (SAT) problem with 3 variables x, y and z. Every variable is defined as a 15-nt single strand DNA (ssDNA) which is immobilized on one spot of the gold surface. We further define SPR reflective intensity changes 0, 0.2 and 2 A.U. caused by changes of molecular weight on surface as Boolean signals False, True and None, respectively. Moreover, False signal represents a positive hybridization reaction via the hydrogen bond that binds the complementary ssDNA conjugating to IgG (150 kDa) by the crosslinker Sulfo-SMPB which can links thiol group labeled on ssDNA and amine group existed on IgG; True signal represents the hybridization reaction that binds the complementary ssDNA-IgG-Antigen which can result in a much larger intensity change. For a SAT problem F = (XT ∪ YF)∩(XF ∪ ZT)∩(YT ∪ ZT), there are 8 possible answers. Therefore, we established a 3-spot array as a set which is immobilized sequence x, y and z. After one calculation, we read out the solution of this set and then regenerate it by injecting 0.05 N sodium hydroxide solution. In this work, we used 200 ng/ml Xc-Human IgG, Yc-Rabbit IgG and Zc-Goat IgG as reaction agents for hybridization which represent False signal. Furthermore, 100 ng/ml Anti-Human IgG, Rabbit IgG and Goat IgG were taken as True signal agents. A full reaction can be completed within 30 minutes at room temperature. The buffer in the study is 1 x phosphate buffered solution (PBS) with 100 mM sodium chloride. The proposed platform has improved drawbacks that occurred in previous researches about DNA computer. Besides, it is provided with abilities a processor should have which are recalculable and realtime measurement so that provides us a novel approach for addressable and reusable diagnosis.
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Krasnoshtanova, Alla, and Alesya Yudina. "PRODUCTION OF ANTIBODIES FROM POULTRY YOLK (IgY) AND INVESTIGATION OF THEIR IMMUNOCHEMICAL PROPERTIES." In GEOLINKS Conference Proceedings. Saima Consult Ltd, 2021. http://dx.doi.org/10.32008/geolinks2021/b1/v3/17.
Повний текст джерелаАнотація:
"A particularly important aspect of immunology is to develop non-invasive methods of obtaining antibodies which could be a great alternative to traditional ones that based on the harmful procedure of isolation of immunoglobulins from animal blood sera. That’s why the extraction of antibodies from poultry egg yolks (IgY) is the most promising. Due to the fact of variation of IgY structural features that determine the definite immunochemical properties, yolk antibodies in comparison with mammalian immunoglobulins (IgG) does not interact with rheumatoid factor (Rf), contribute to the activation of the complement system, bind to the Fc-receptor (FcR), and also has weak cross-reactivity, which confirms the possibility of their widespread use in medicine and food. Also the presence of phylogenetic distance between chickens and mammalians guarantees immune response against conservative mammalian protein molecules which is highly important for the creation of new generation test systems. The aim of this work is to develop a selective method of producing high-purity immunoglobulin Y preparations from the yolk of chicken eggs. There were adopted selective conditions of isolation of IgY under spontaneous thawing procedure at the room temperature of firstly frozen yolk solution in a sodium-phosphate buffer mixed with water (pH 5.0) in a ratio of 1:6, which leads to receiving a water-soluble fraction further precipitated with the sodium chloride at a concentration of 10% of the solution mass and subsequently concentrated using ultrafiltration with membrane UAM-10, that allows achieving the content of IgY not less than 95% per dry substance in immunoglobulin fraction. It is possible to produce a protein fraction with a protein content of at least 9 g/l. The purity of the immunoglobulin fraction was verified using polyacrylamide gel electrophoresis. The presence of a light chain in the IgY solution was proved to be a low-molecular compound using the method of gel-filtration-chromatography. The immunological activity of IgY was studied with respect to bovine serum albumin (BSA) as an antigen. The enzymatic resistance of IgY against proteolytic enzymes was tested in area of the gastrointestinal tract."
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Imura, J., N. Suzuki, K. Higashi, M. Tubokura, and K. Shirasawa. "EFFECTS OF PLASMA MEMBRANE GLYCOPROTEIN OF PLATELETS ON THE AGGREGATION ACTIVITY OF THE STORED CELLS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644593.
Повний текст джерелаАнотація:
Platelet aggregation activity is gradually reduced depending on the duration of storage. Platelet membrane glycoprotein IIb/IIIa (GPIIb/IIIa) complex is intimately related to the aggregation activity. We intended, therefore, to analyse a sequential change in plasma membrane glycoprotein of stored platelets by means of flow cytometry (FCM). On this occasion, aggregation activity of the platelets was also studied. Concentrated human platelets (150×104 cell/μl) were stored in the bag containing citrate-phosphate-dextrose at 22 °C for 24 to 72 hours. The bags were either kept in a flat position without agitation or continuosly stirred by a tumbler agitator (6rpm), or a flat bed rotator (30rpm). At the beginning of each experiment, fresh platelets separated from healthy donor were used as control group. The remaining platelets were washed twice with the 0.38% sodium-citrate dissolved in the lOmM of PBS. After incubation of the suspended platelets in the Tyrode's buffer solution at 37 °C for 30 minutes, they were fixed with 1% paraformaldehyde at 4 C for 2 hours, and were then incubated with anti-human GP IIb/IIIa mouse monoclonal antibody (5μg/ml) at 37 °C for 1 hour. The platelets, thus treated with primary antibody, had undergone further incubation with fluorescein-conjugated goat anti-inouse IgG immunoglobulin at 37°C for 1 hour. After analysis of labelled platelets on the Coulter EPICS V, the positive rate was estimated by counting 5×104 cells. In each group, aggregation activity of platelets induced by ADP (100μM) was measured by an aggregometer.The positive rate was significantly decreased in the stored platelets compared with those in the control group. In addition, the positive rate was more decreased in the non-agitated group than in the agitated group. No difference, however, occurred in the rate from the agitated groups. Moreover, the aggregation activity in each group was well compatible with the positive rate from FCM.It is finally suggested that the decrease in aggregation activity of the stored platelet is due to the reduction in the functioning receptor sides of GPIIb/IIIa on the platelet surface.
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Mihalcea, Elena, Gabi Drochioiu, Stefania-Claudia Jitaru, Violeta Mangalagiu, and Robert �Vasile Gradinaru. "PROTEIN AND PEPTIDE DETERMINATION BASED ON THE MODIFIED BIURET PROCEDURE: IMPLICATIONS FOR VARIOUS BIOTECHNOLOGIES." In 22nd SGEM International Multidisciplinary Scientific GeoConference 2022. STEF92 Technology, 2022. http://dx.doi.org/10.5593/sgem2022/6.1/s25.14.
Повний текст джерелаАнотація:
Spectrophotometric methods for total protein analysis are generally simple, rapid and sensitive. Such sensitive protein assays may have applications in forensic science, in the detection of protein contaminants in drugs and in a number of other applications of research interest. Biuret reaction with proteins and peptides is widely used in clinical and biological laboratories. In this work, instead of copper sulphate, sodium hydroxide and Seignette salt, we used insoluble copper phosphate, potassium or sodium hydroxide and ethyl alcohol for the preparation of the biuret reagent. Absorbance of the biuret complex was recorded both at 219-230 nm (after dilution) and around 550 nm against a reagent blank. Amino acid interference was investigated around 550 nm at the same concentration as proteins. The sensitivity of the method at 226 nm was greater than those of other spectrophotometric assays (old biuret method, Lowry, and BCA) with a LOD of about 0.5 �g mL?1 BSA. The new variants of the biuret method for total protein analysis eliminate the need for precise reagent addition and vortexing inherent in the widely used Lowry method, providing flexibility of application. The method developed, which uses an alkaline-alcoholic reagent and insoluble copper phosphate, is simple, rapid, reproducible and sensitive; it is not influenced by detergents, solvents and buffers containing ammonium and is flexible enough to change the analytical protocol when necessary. A discussion was made on the applications of protein and peptide determination with the new biuret assay.
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Oka, Taiki, Ruri Hidema, Hiroshi Suzuki, and Yoshiyuki Komoda. "Effects of Contraction Ratio on Elastic Instability of Hyaluronate Solution in a Micro Channel." In ASME/JSME/KSME 2015 Joint Fluids Engineering Conference. American Society of Mechanical Engineers, 2015. http://dx.doi.org/10.1115/ajkfluids2015-18556.
Повний текст джерелаАнотація:
Flow behaviors of sodium hyaluronate (HA-Na) in water solution and in phosphate buffered saline (PBS) solution as a viscoelastic fluids in planer abrupt contraction-expansion channels has been observed in this study. Especially, the effect of the geometry of the flow path on the flow behavior was focused on. The corner vortices in the corner of the upper region in the abrupt contraction-expansion channels were also analyzed to quantify the flow characteristics. The elasticity numbers of the solution, which is affected by rheological properties of the solution and the channel geometry had a big influence on the fluidity, that is, stable or unstable, when the concentration of the solution in lower. It was concluded that such stable and unstable flows are categorized on Wissenberg-Reynolds number space.