Comparison of pH and ionic strength dependence of interactions between monoclonal antibodies and bovine beta-Lactoglobulin

被引：10

作者：

Kamata, N

Enomoto, A

Ishida, S

Nakamura, K

Kurisaki, JI

Kaminogawa, S

机构：

[1] NATL INST ANIM IND, INASHIKI, IBARAKI 305, JAPAN

[2] UNIV TOKYO, DEPT APPL BIOL CHEM, DIV AGR & AGR LIFE SCI, BUNKYO KU, TOKYO 113, JAPAN

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1996年 / 60卷 / 01期

关键词：

antigen-antibody reactions; monoclonal antibodies; enzyme-linked immunosorbent assay; pH dependence; ionic strength dependence;

D O I：

10.1271/bbb.60.25

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：

A panel of 13 monoclonal antibodies (mAbs) against distinct determinants on bovine beta-lactoglobulin, a model protein antigen, were examined and compared for their ability to bind and desorb from the antigen at differing pHs and ionic strengths by an enzyme-linked immunosorbent assay and elution assay. Among them, mAb 61Cl was found to be highly sensitive to the pH, and 3 in 4 mAbs directed to the region 42-56 also strongly depended on the change in ionic strength. Because of the large proportion of charged amino acid residues in the region 42-56, the electrostatic forces are considered to be more predominant than the hydrophobic interactions in the latter antigen-antibody reactions, thereby resulting in their high sensitivity to the ionic strength.

引用

页码：25 / 29

页数：5

共 21 条

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