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An in vitro system for studying the kinetics of interchain disulfide bond formation in immunoglobulin G.

作者信息

Petersen J G, Dorrington K J

出版信息

J Biol Chem. 1974 Sep 10;249(17):5633-41.

PMID:4212934
Abstract
摘要

相似文献

1
An in vitro system for studying the kinetics of interchain disulfide bond formation in immunoglobulin G.一种用于研究免疫球蛋白G中链间二硫键形成动力学的体外系统。
J Biol Chem. 1974 Sep 10;249(17):5633-41.
2
Equilibrium and kinetic aspects of subunit association in immunoglobulin G.免疫球蛋白G中亚基缔合的平衡和动力学方面
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Dilatometric studies of the denaturation of immunoglobulin G by guanidinium chloride.用氯化胍对免疫球蛋白G变性的膨胀计研究。
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The structure and function of immunoglobulin domains. II. The importance of interchain disulfide bonds and the possible role of molecular flexibility in the interaction between immunoglobulin G and complement.免疫球蛋白结构域的结构与功能。II. 链间二硫键的重要性以及分子柔性在免疫球蛋白G与补体相互作用中的可能作用。
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Human IgG is substrate for the thioredoxin system: differential cleavage pattern of interchain disulfide bridges in IgG subclasses.人免疫球蛋白G是硫氧还蛋白系统的底物:免疫球蛋白G亚类中链间二硫键的差异裂解模式。
Mol Immunol. 1997 Jul;34(10):709-17. doi: 10.1016/s0161-5890(97)00092-8.
6
Interchain disulfide bonds in immunoglobulins: analysis by two-dimensional polyacrylamide-gel electrophoresis.
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7
Formation of interchain disulfide bonds in Bence Jones proteins and immunoglobulins.
J Biochem. 1976 Jan;79(1):91-105. doi: 10.1093/oxfordjournals.jbchem.a131062.
8
A kinetic study in vitro of the reoxidation of interchain disulfide bonds in a human immunoglobulin IgGLk. Correlation between sulfhydryl disappearance and intermediates in covalent assembly of H2L2.人免疫球蛋白IgGLk中链间二硫键再氧化的体外动力学研究。巯基消失与H2L2共价组装中间体之间的相关性。
Proc Natl Acad Sci U S A. 1975 Jan;72(1):353-7. doi: 10.1073/pnas.72.1.353.
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Dissociation of fibrinogen and fibrin peptide chains by partial cleavage of disulfide bonds.
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Release of a low molecular weight Fc-like fragment on reduction of water-insoluble IgG myeloma proteins.还原水不溶性IgG骨髓瘤蛋白时低分子量Fc样片段的释放。
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On-column disulfide bond formation of monoclonal antibodies during Protein A chromatography eliminates low molecular weight species and rescues reduced antibodies.
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A New Classification System for IgG4 Autoantibodies.一种新的 IgG4 自身抗体分类系统。
Front Immunol. 2018 Feb 12;9:97. doi: 10.3389/fimmu.2018.00097. eCollection 2018.
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Disulfide bond structures of IgG molecules: structural variations, chemical modifications and possible impacts to stability and biological function.IgG 分子的二硫键结构:结构变异、化学修饰以及对稳定性和生物学功能的可能影响。
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Normal human immunoglobulin G4 is bispecific: it has two different antigen-combining sites.正常人类免疫球蛋白G4具有双特异性:它有两个不同的抗原结合位点。
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Intrachain disulfide bond in the core hinge region of human IgG4.人IgG4核心铰链区的链内二硫键
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