EXPRESSION OF MULTIVALENCY IN THE AFFINITY CHROMATOGRAPHY OF ANTIBODIES - APPENDIX - DERIVATION AND EVALUATION OF EQUATIONS FOR INDEPENDENT BIVALENT INTERACTING SYSTEMS IN QUANTITATIVE AFFINITY CHROMATOGRAPHY

被引：56

作者：

EILAT, D ^{[1
]}

CHAIKEN, IM ^{[1
]}

MCCORMICK, WM ^{[1
]}

机构：

[1] NIAMDD,CHEM BIOL LAB,BETHESDA,MD 20014

来源：

BIOCHEMISTRY | 1979年 / 18卷 / 05期

关键词：

D O I：

10.1021/bi00572a008

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 expression of multivalency in the interaction of antibody with immobilized antigen was evaluated by quantitative affinity chromatography. Zones of radioisotopically labeled bivalent immunoglobulin A monomer derived from the myeloma protein TEPC 15 were eluted from columns of phosphorylcholine-Sepharose both in the absence and presence of competing soluble phosphorylcholine. At sufficient immobilized phosphorylcholine concentration, the variation of elution volume of bivalent monomer with soluble ligand was found to deviate from that observed for the univalent binding of the corresponding Fab fragment. In addition, the apparent. © 1979, American Chemical Society. All rights reserved.

引用

页码：790 / 795

页数：6

共 18 条

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[7] EVALUATION OF QUANTITATIVE AFFINITY CHROMATOGRAPHY BY COMPARISON WITH KINETIC AND EQUILIBRIUM DIALYSIS METHODS FOR ANALYSIS OF NUCLEOTIDE BINDING TO STAPHYLOCOCCAL NUCLEASE
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