SUSCEPTIBILITY OF MONOCLONAL IGG PARAPROTEINS TO PLASMIC CLEAVAGE USING GLYCERIN STABILIZED HUMAN PLASMIN
SUSCEPTIBILITY OF MONOCLONAL IGG PARAPROTEINS TO PLASMIC CLEAVAGE USING GLYCERIN STABILIZED HUMAN PLASMIN
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DOI：
10.1006/bbrc.1994.1937
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发表时间：
1994-07-15
影响因子：
3.1
通讯作者：
CHUBA, JV
中科院分区：
文献类型：
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作者：
CHUBA, JV
为了进一步阐明纤溶酶-免疫球蛋白的相互作用，描述了一种简单的程序，该程序允许从人血清中分离出48株单克隆性免疫球蛋白以分析其对血浆切割的敏感性。除了阳极型Fc和阴极型Fab片段外，联合免疫电泳法还显示在许多Ig G亚类1分离株中有瞬时的阳极带和Fab-片段亚裂解。释放的带有独特型决定簇的Fab片段的亚切割表明，纤溶酶在导致免疫调节抗独特型网络的“独特型加工”中可能起到辅助作用。内源性纤溶酶对免疫球蛋白的裂解也表明纤溶酶在免疫球蛋白的“稳态”代谢中可能起着积极的作用。(C)1994年学术出版社。
To shed further light on plasmin-IgG interactions a simple procedure is described that permitted 48 monoclonal IgG isolates from human serum to be profiled for their susceptibility to plasmic cleavage. In addition to anodal Fc and cathodal Fab fragments, combined immunoelectrophoresis electrophoresis revealed transient anodal banding, as well as Fab-fragment subcleavage in many of the IgG subclass-1 isolates. The subcleavage of released Fab fragments, which bear the idiotype determinants, points to a possible ancillary role of plasmin in ''idiotype processing'' leading to immunoregulatory antiidiotype networks. The cleavage of IgG by endogenous plasmin also points to a possible active role of plasmin in the ''steady-state'' metabolism of IgG. (C) 1994 Academic Press, Inc.