ANTIGEN-SPECIFICITY OF ANTICOLIPASE MONOCLONAL-ANTIBODIES - CHARACTERIZATION OF COLIPASE-FAB COMPLEXES USING GEL-FILTRATION HIGH-PERFORMANCE LIQUID-CHROMATOGRAPHY

被引：3

作者：

RUGANI, N ^{[1
]}

DEZAN, C ^{[1
]}

BELLON, B ^{[1
]}

SARDA, L ^{[1
]}

机构：

[1] FAC ST CHARLES, INST CHIM BIOL, PL VICTOR HUGO, F-13331 MARSEILLE 3, FRANCE

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 177卷 / 02期

关键词：

D O I：

10.1016/0006-291X(91)91848-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The epitope specificity of eight mouse monoclonal antiporcine procolipase antibodies (MAbs) was characterized on the basis of their competitive binding with antigen. Binary and ternary Fab-colipase complexes formed between antibody and porcine procolipase or its trypsin activated derivative were identified using gel filtration HPLC. The eight MAbs were divided in two groups that recognized overlapping epitopes located in distinct antigenic regions on procolipase. The gel filtration HPLC technique allowed to characterize two MAbs which did not react with solid-phase coupled antigen. Three MAbs formed Fab-antigen complexes with procolipase and not with activated colipase which suggests that epitopes recognized by these MAbs involve residues of the N-terminal pentapeptide of procolipase. © 1991.

引用

页码：726 / 733

页数：8

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