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[分子间静电协同相互作用导致人单克隆免疫球蛋白M冷沉淀的作用]

[The role of intermolecular electrostatic cooperative interactions causing cryoprecipitation of human monoclonal immunoglobin M].

作者信息

Kosarev I V, Surovtsev V I, Zav'ialov V P

出版信息

Bioorg Khim. 1985 Jun;11(6):745-52.

PMID:3929795
Abstract

A chemical modification of carboxylic groups of monoclonal human cryoglobulin M has been studied. The modification by a chromophoric carbodiimide was accompanied by complete loss of IgM cryoprecipitating properties. The number of carboxylic groups important for biological activity was estimated by the Tsou method and found to be 2. The cryoprecipitation dependence on ionic strength has been investigated and the number of ions per binding site isolated upon formation of intermolecular ion couples has been estimated. Mechanism of cryoprecipitation stipulated by intermolecular cooperative electrostatic interactions is proposed.

摘要

对人单克隆冷球蛋白M的羧基进行了化学修饰研究。用发色碳二亚胺进行修饰时,IgM的冷沉淀特性完全丧失。采用邹氏方法估算了对生物活性重要的羧基数量,发现为2个。研究了冷沉淀对离子强度的依赖性,并估算了分子间离子对形成时每个结合位点分离出的离子数量。提出了由分子间协同静电相互作用规定的冷沉淀机制。

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