EPITOPE MAPPING AND BINDING-KINETICS OF MONOCLONAL-ANTIBODIES STUDIED BY REAL-TIME BIOSPECIFIC INTERACTION ANALYSIS USING SURFACE-PLASMON RESONANCE

被引：64

作者：

JOHNE, B ^{[1
]}

GADNELL, M ^{[1
]}

HANSEN, K ^{[1
]}

机构：

[1] PHARMACIA BIOSENSOR AB,UPPSALA,SWEDEN

来源：

JOURNAL OF IMMUNOLOGICAL METHODS | 1993年 / 160卷 / 02期

关键词：

MONOCLONAL ANTIBODY; MYOGLOBIN; IMMUNOASSAY; BIOSENSOR; BIACORE; REAL TIME BIOSPECIFIC INTERACTION ANALYSIS;

D O I：

10.1016/0022-1759(93)90177-9

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The interaction between human heart myoglobin and ten specific monoclonal antibodies was investigated with a new biosensor technology, real time biospecific interaction analysis (RT BIA), using surface plasmon resonance. Analysis of association and dissociation kinetics was monitored in real time, with unlabelled reactants. Antibody isotyping was rapid and simple. Epitope mapping with RT BIA confirmed, with substantial time saving, the sum of results obtained in conventional labelled systems. Monoclonal antibodies with four different epitope specificities and optimal binding function were selected for a myoglobin sandwich assay with enhanced sensitivity. BIAcore can be used directly as a diagnostic tool, or as an analytical tool in immunoassay development.

引用

页码：191 / 198

页数：8

共 29 条

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