Готові списки джерел за темами / Isoelectric focussing

Добірка наукової літератури з теми "Isoelectric focussing"

Автор: Grafiati
Опубліковано: 10 грудня 2022
Оновлено: 28 січня 2023

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Статті в журналах з теми "Isoelectric focussing"

1

Houston, B., and C. Goddard. "Molecular forms of growth hormone in the chicken pituitary gland." Journal of Endocrinology 116, no. 1 (January 1988): 35—NP. http://dx.doi.org/10.1677/joe.0.1160035.

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ABSTRACT Different forms of GH present in freshly prepared homogenates of chicken pituitary were analysed by high-performance gel permeation chromatography and by immunoblotting following sodium dodecylsulphate polyacrylamide gel electrophoresis, non-denaturing polyacrylamide gel electrophoresis and isoelectric focussing. Chicken GH was found to occur mainly in a monomeric form with a relative molecular mass of 23 500 together with small amounts of interchain disulphide-linked oligomers. No evidence was obtained for proteolytically modified forms of GH nor for a form analogous to the 20K variant of human GH. Isoelectric focussing resolved ten distinct charge variants of chicken GH with isoelectric points between 8·45 and 6·0. The predominant charge variant (pI = 7·85) was present in pituitaries of birds of both sexes at all ages examined (3–114 days) whereas the more acidic forms were not apparent until after day 13. These findings indicate that the chicken pituitary contains different forms of GH, some of which may be developmentally regulated. J. Endocr. (1988) 116, 35–41
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2

Minshull, Thomas C., Amanda Wood, David Roberts, Christine Hallam, Joshua Lewis, Adetola Orekoya, and David Gervais. "Determination of extent of PEGylation using denaturing capillary isoelectric focussing." Analytical Biochemistry 611 (December 2020): 113953. http://dx.doi.org/10.1016/j.ab.2020.113953.

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3

Ataman, Can, Ufuk Çelik, and Hartmut Rehbein. "Identification of some Aegean fish species by native isoelectric focussing." European Food Research and Technology 222, no. 1-2 (October 13, 2005): 99–104. http://dx.doi.org/10.1007/s00217-005-0149-0.

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4

Miao, J. K., X. Q. Yu, and M. Z. Huang. "Study of the Isoelectric Point (IEP) and Isoelectric Point Distribution (IEPD) of Photographic Gelatinwith Isoelectric Focussing on Flat Bed Polyacrylamide Gel." Journal of Photographic Science 40, no. 5-6 (September 1992): 165–67. http://dx.doi.org/10.1080/00223638.1992.11737197.

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5

Pioselli, Barbara, Caroline Munro, Andrea Raab, Christian L. Deitrich, Kriangsak Songsrirote, Jörg Feldmann, and Jane Thomas-Oates. "Denaturing and non-denaturing microsolution isoelectric focussing to mine the metalloproteome." Metallomics 1, no. 6 (2009): 501. http://dx.doi.org/10.1039/b903607e.

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6

Houston, B., I. E. O'Neill, M. A. Mitchell, and C. Goddard. "Purification and biological activity of a single charge isomer of pituitary-derived chicken growth hormone." Journal of Endocrinology 125, no. 2 (May 1990): 207–15. http://dx.doi.org/10.1677/joe.0.1250207.

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ABSTRACT The chicken pituitary gland contains a number of naturally occurring, developmentally regulated forms of GH which have identical molecular weights but differ in their isoelectric points. In order to characterize their biological properties, each must be separated from non-GH proteins and other forms of GH. Chicken GH (cGH) was separated from other pituitary proteins by immunoaffinity chromatography using an anti-GH monoclonal antibody covalently linked to Sepharose 4B. The cGH eluted from this column as a single peak and migrated as a single band during sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), but showed multiple bands on isoelectric focussing. This material was chromatographed on a high-performance cation exchange column, and separation of charge isomers was monitored by a combination of isoelectric focussing and immunoblotting. Chicken GH eluted from this column in two distinct peaks. The minor peak (cGH P1) contained an isomer with an isoelectric point of 6·86 and the major peak (cGH P2) an isomer with an isoelectric point of 7·52. Each isomer migrated as a single band during isoelectric focussing and SDS-PAGE (Mr = 23 500), and as a single peak during high-performance gel permeation chromatography and reverse-phase high-performance liquid chromatography. Analysis of cGH P2 through 30 cycles in a gas-phase microsequencer gave an amino acid sequence identical to that predicted by translation of the GH complementary DNA nucleotide sequence. This single charge isomer increased the rate of lipolysis in chicken adipose tissue explants by about fourfold and was able to displace 125I-labelled cGH from binding sites in liver membranes with a dissociation constant of about 4 nmol/l. The output of insulin-like growth factor-I by hepatocytes in culture was increased from a basal rate of 50·4±11·6 (mean ± s.e.m.) to 787·9 ± 98·6 pg/6 × 106 cells per 48 h by two separate pulses of 1 μg cGH P2/ml. An i.v. injection of cGH P2 (15 μg/kg body weight) decreased the thyroxine:tri-iodothyronine ratio in serum of adult hens from 15·71 to 4·44, indicating an increase in 5′-monodeiodinase activity. These results demonstrate that the single most abundant charge isomer of chicken pituitary GH is likely to contain all the biological activity ascribed to the hormone. Journal of Endocrinology (1990) 125, 207–215
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7

Getliffe, K. A., L. C. Ward, and R. W. Shepherd. "Identification of cystic fibrosis homozygotes and heterozygotes by isoelectric focussing of serum proteins." Journal of Inherited Metabolic Disease 9, no. 4 (December 1986): 348–56. http://dx.doi.org/10.1007/bf01800484.

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8

Bodinet, C., N. Beuscher, and L. Kopanski. "Purification of Immunologically Active Glycoproteins fromBaptisia tinctoriaRoots by Affinity Chromatography and Isoelectric Focussing." Planta Medica 55, no. 07 (December 1989): 659. http://dx.doi.org/10.1055/s-2006-962249.

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9

Kang, Sungzong, and Julian Niemetz. "Purification of Human Brain Tissue Factor." Thrombosis and Haemostasis 59, no. 03 (1988): 400–403. http://dx.doi.org/10.1055/s-0038-1647504.

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SummaryTissue factor (thromboplastin or Factor III), a glycoprotein cofactor, is required for Factor VII to express its catalytic activity, thereby initiating the extrinsic as well as intrinsic pathway of blood coagulation. Human brain tissue factor was purified 2,500-fold to 98% homogeneity from 2% Tiiton X-100 extraction of acetone dried brain powder with an overall yield of 36%. The method was based upon affinity chromatography utilizing the high affinity binding of tissue factor to Factor VII noncovalently complexed to immobilized anti-Factor VII-agarose beads. The apparent molecular weight of the purified tissue factor is 45,000 as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and its isoelectric point is 4.8–5.1 by column chromatofocussing and flat bed agarose isoelectric focussing.
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10

Anderson, Carrie L., Yang Wang, and Richard R. Rustandi. "Applications of imaged capillary isoelectric focussing technique in development of biopharmaceutical glycoprotein-based products." ELECTROPHORESIS 33, no. 11 (June 2012): 1538–44. http://dx.doi.org/10.1002/elps.201100611.

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Дисертації з теми "Isoelectric focussing"

1

Guttridge, Martin Gordon. "An improved method for one-dimensional isoelectric focussing of HLA class 1 molecules and its clinical application." Thesis, University of the West of England, Bristol, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.293274.

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Частини книг з теми "Isoelectric focussing"

1

Arnold, G., M. J. Prata, A. Amorim, J. Kömpf, and H. Ritter. "Subtyping of coagulation factor XIIIA by Isoelectric focussing." In Advances in Forensic Haemogenetics, 605–7. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78782-9_170.

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2

Phillips, C. P. "Phenotyping Adenosine Deaminase using Ultra-Thin Isoelectric Focussing." In Advances in Forensic Haemogenetics, 108–12. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73330-7_21.

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3

Bickelmann, U. "Pedigree of German Oat Cultivars and Their Identification by Isoelectric Focussing." In Proceedings of the Second International Oats Conference, 145. Dordrecht: Springer Netherlands, 1986. http://dx.doi.org/10.1007/978-94-009-4408-4_32.

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4

"Chapter 7 The Dynamics of Isoelectric Focussing." In The Proteome Revisited Theory and Practice of all Relevant Electrophoretic Steps, 81–84. Elsevier, 2001. http://dx.doi.org/10.1016/s0301-4770(01)80039-7.

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5

"Chapter 11 Limitations of the Method of Isoelectric Focussing." In The Proteome Revisited Theory and Practice of all Relevant Electrophoretic Steps, 109–19. Elsevier, 2001. http://dx.doi.org/10.1016/s0301-4770(01)80043-9.

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6

"Chapter 12 Conventional Isoelectric Focussing in Gel Slabs and Capillaries and Immobilised pH Gradients." In The Proteome Revisited Theory and Practice of all Relevant Electrophoretic Steps, 123–215. Elsevier, 2001. http://dx.doi.org/10.1016/s0301-4770(01)80044-0.

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Тези доповідей конференцій з теми "Isoelectric focussing"

1

Giridharan, M. G., and Anantha Krishnan. "An Implicit Numerical Model for Electrophoretic Systems." In ASME 1998 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 1998. http://dx.doi.org/10.1115/imece1998-1223.

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Abstract An implicit finite-volume approach has been developed to solve the equations governing the electrophoretic process. The numerical procedure involves the sequential solution of the species conservation ionization equilibria and electro-neutrality equations in an iterative fashion until convergence. This implicit procedure is numerically stable and allows for faster steady-state solutions or larger time steps for time-accurate simulations. Temporal evolutions of pH, species concentrations and electrolyte conductivity are predicted. The results obtained using various higher order numerical schemes are compared and assessed. Results are presented for the isoelectric focussing, moving boundary electrophoresis, and capillary electrophoresis of amino acids and a protein. The predictions for the isoelectric focussing of albumin protein are in qualitative agreement with published experimental data.
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2

Rathjen, Deborah A., and Carolyn L. Geczy. "PRODUCTION AND CHARACTERISATION OF A MONOCLONAL ANTIBODY AGAINST HUMAN ANTI-THROMBIN III." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644358.

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To study the role of anticoagulants, particularly antithrombin III (AT III) and heparin, on the activation of coagulation by monocytes/macrophages which have been stimulated with a soluble lymphocyte activation product, macrophage procoagulant inducing factor, we have prepared monoclonal antibodies (MAbs) to human AT III.In fusion experiments, in contrast to wells containing peritoneal feeder cells, positive hybrids were only found in wells containing medium conditioned by the macrophage cell line J774 (Rathjen and Geczy, 1986). Of 5 hybrids which initially produced antibody, only one hybrid, showed stable Ab production. The MAb, designated 22/23, was not cross-reactive with either 1 antitrypsin or ovalbumin and did not inhibit the biological activity of AT III in chromogenic assays which measured inhibition of thrombin and Factor Xa by AT III. An immunoadsorbent prepared using MAb 22/23 depleted AT III activity from a purified AT III preparation. Reduction and alkylat ion of the disulphide bonds of the protein portion of AT III completely abbrogated MAb binding indicating that the native configuration of AT III was important. Isoelectric focussing of AT III, followed by transfer of the focussed protein to nitrocellulose by diffusion and probing with MAb 22/23, revealed at least 8 bands in the region of pH 5.2 to 5.85. Coomassie blue staining of a gel run in parallel showed 9 bands in this region. The MAb provides a useful tool for the detection of AT III on both cultured cells (bovine aortic endothelial cells are positive by immunofluorescence) and tissue sections.Rathjen, D.A. and Geczy, C.L. Hybridomo. 5s 255-261 (1986)
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