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The effect of alternate substrates and substrate concentration on the antibody-mediated inhibition of horseradish peroxidase.

Abstract：

:Inhibition of the catalytic activity of horseradish peroxidase by rabbit antisera was measured using alternate enzyme substrates. The same general inhibition curve patterns were obtained regardless of the electron donor or hydroperoxide used. In all cases typical biphasic inhibition patterns were found and complete inhibition of enzyme activity was never observed. Measurement of the degree of inhibition as a function of substrate concn revealed a dependence of anticatalytic activity on hydroperoxide concn. As the concn of hydrogen peroxide in the assay mixture increased, there was a corresponding increase in the inhibition observed. On the other hand, the degree of inhibition was not dependent on the concn of electron donor (dianisidine) in the assay mixture. Spectrophotometric experiments with an electron donor analogue demonstrated that antibodies do not inhibit peroxidase activity by excluding electron donor molecules from enzyme binding sites. The results have suggested possible mechanisms for the antibody-mediated inhibition of peroxidase activity.

journal_name

Mol Immunol

journal_title

Molecular immunology

authors

Clark SK Jr,Conroy JM,Harris PJ

doi

10.1016/0161-5890(83)90169-4

subject

Has Abstract

pub_date

1983-12-01 00:00:00

pages

1379-84

issue

12

eissn

0161-5890

issn

1872-9142

journal_volume

20

pub_type

杂志文章

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