INACTIVATION OF ALCOHOL-DEHYDROGENASE BY 3-BUTYN-1-OL

被引：19

作者：

ALSTON, TA

MELA, L

BRIGHT, HJ

机构：

[1] UNIV PENN,SCH MED,DEPT BIOCHEM & BIOPHYS,PHILADELPHIA,PA 19104

[2] UNIV PENN,SCH MED,DEPT SURG,PHILADELPHIA,PA 19104

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 1979年 / 197卷 / 02期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/0003-9861(79)90275-3

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：

Horse liver and yeast alcohol dehydrogenases are rapidly inactivated during their catalysis of the oxidation of 3-butyn-1-ol. In the case of the horse liver enzyme, the inactivation is secondary to covalent modification of the apoenzyme by an electrophilic product that accumulates in the reaction solution and that can also react with water, glutathione, and other enzymes. The modified protein exhibits enhanced ultraviolet absorbance, which is not bleached upon dialysis of the denatured enzyme at pH 7.4 for 24 h. The inactivation by 3-butyn-1-ol is more rapid than that which is afforded by the related alcohols 2-propyn-1-ol and 2-propen-1-ol under identical conditions and no inactivation is seen upon incubation with 3-hydroxypropanoic nitrile plus nicotinamide-adenine dinucleotide. © 1979.

引用

页码：516 / 523

页数：8

共 37 条

[1] CHEMOTHERAPEUTIC ACTION OF A CYCLIC NITROGEN MUSTARD PHOSPHAMIDE ESTER (B 518-ASTA) IN EXPERIMENTAL TUMOURS OF THE RAT [J].