A SPECTRAL STUDY OF THE BIOCHEMICAL REACTIONS OF PHOSPHINE WITH VARIOUS HEMOPROTEINS

被引：19

作者：

CHAUDHRY, MQ ^{[1
]}

PRICE, NR ^{[1
]}

机构：

[1] AGR DEV & ADVISORY SERV, CENT SCI LAB, SLOUGH SL3 7HJ, BERKS, ENGLAND

来源：

PESTICIDE BIOCHEMISTRY AND PHYSIOLOGY | 1990年 / 36卷 / 01期

关键词：

D O I：

10.1016/0048-3575(90)90015-T

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 spectral changes in haemoglobin, myoglobin, catalase, and peroxidase were studied as part of an investigation of the biochemical mode of action of phosphine. Slow deoxygenation of both the oxygen-carrier proteins, haemoglobin, and myoglobin resulted from treatment with phophine while there was no significant spectral change in either catalase or peroxidase and there was no direct inhibition of catalase activity. Phosphine appeared to have higher affinity for oxygen than haemoglobin or myoglobin. The toxic action of phosphine based on its reducing and deoxygenating properties is suggested. © 1990.

引用

页码：14 / 21

页数：8

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