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聚乙二醇偶联免疫球蛋白G的物理化学和生物学性质

Physicochemical and biological properties of poly(ethylene glycol)-coupled immunoglobulin G.

作者信息

Suzuki T, Kanbara N, Tomono T, Hayashi N, Shinohara I

出版信息

Biochim Biophys Acta. 1984 Jul 31;788(2):248-55. doi: 10.1016/0167-4838(84)90268-1.

Abstract

In order to develop a new intravenous immunoglobulin G (IgG), IgG was covalently coupled to poly(ethylene glycol) previously activated by cyanuric chloride. The poly(ethylene glycol) coupled IgG obtained was studied for physicochemical and biological properties such as molecular structure, size-exclusion chromatographic behaviour, surface activity, interfacial aggregability, heat aggregability inducing nonspecific complement activation, and antigen-binding activity. The poly(ethylene glycol) coupling to IgG increased the apparent Stokes' radius and the surface activity of IgG and stabilized IgG on heating and/or on exposure to interface, while no structural denaturation of IgG was observed. The suppressed nonspecific aggregability was interpreted mainly by difficulty in association between the modified IgG molecules. These results indicated the use of the poly(ethylene glycol)-coupled IgG as an intravenous preparation and also as an additive stabilizing intact IgG for intravenous use.

摘要

为了开发一种新型静脉注射免疫球蛋白G(IgG),将IgG与先前用三聚氯氰活化的聚乙二醇共价偶联。对获得的聚乙二醇偶联IgG进行了物理化学和生物学性质研究,如分子结构、尺寸排阻色谱行为、表面活性、界面聚集性、诱导非特异性补体激活的热聚集性以及抗原结合活性。聚乙二醇与IgG的偶联增加了IgG的表观斯托克斯半径和表面活性,并在加热和/或暴露于界面时使IgG稳定,同时未观察到IgG的结构变性。非特异性聚集性的抑制主要归因于修饰后的IgG分子之间难以缔合。这些结果表明聚乙二醇偶联IgG可作为静脉制剂使用,也可作为一种添加剂用于稳定静脉注射用的完整IgG。

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