人多形核白细胞弹性蛋白酶对人免疫球蛋白G的蛋白水解作用产生具有体外生物活性的Fc片段。
Proteolysis of human IgG by human polymorphonuclear leucocyte elastase produces an Fc fragment with in vitro biological activity.
作者信息
Prince H E, Folds J D, Spitznagel J K
出版信息
Clin Exp Immunol. 1979 Jul;37(1):162-8.
Abstract
The Fc fragment derived by proteolysis of human IgG by human polymorphonuclear leucocyte (PMN) elastase was tested for in vitro biological activity. This fragment could attach to the specific IgG receptor of Staphylococcus aureus Cowan I cells (protein A) and could be eluted from the cells with dissociating buffer. Taking advantage of this attachment, it was shown that the Fc fragment is capable of attaching to the antigen-combining site of an IgM rheumatoid factor and can bind to the Fc receptor of human PMN. A similar fragment produced in vivo at sites of inflammation could play a role in regulating the inflammatory response.
摘要
对人多形核白细胞（PMN）弹性蛋白酶水解人IgG产生的Fc片段进行了体外生物活性测试。该片段可附着于金黄色葡萄球菌考恩I型细胞（蛋白A）的特异性IgG受体，并可用解离缓冲液从细胞上洗脱下来。利用这种附着作用，结果表明Fc片段能够附着于IgM类风湿因子的抗原结合位点，并能与人PMN的Fc受体结合。在炎症部位体内产生的类似片段可能在调节炎症反应中发挥作用。
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