Inhibition of rat liver rhodanese by di-, tricarboxylic, and alpha-keto acids.

Abstract:

:Rat liver rhodanese [EC 2.8.1.1] purified by ammonium sulfate fractionation, CM-cellulose and Sephadex G-200 chromatography yielded two active fractions (I & II). Their molecular weights were estimated to be 1.75 X 10(4) (I) and 1.26 X 10(4) (II) by the gel filtration method. Kinetic studies revealed that Fraction I rat liver rhodanese catalyzes thiocyanate formation from thiosulfate and cyanide by a double displacement mechanism. Carboxylic acids such as DL-isocitric, citric malic, pyruvic, and oxaloacetic acid were competitive inhibitors with respect to thiosulfate, whereas fumaric, succinic, and alpha-ketoglutaric acids were noncompetitive inhibitors with respect ot thiosulfate. Incubation of mitochondria with sulfate and alpha-ketoglutaric acid caused a significant decrease in rhodanese activity.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Oi S

doi

10.1093/oxfordjournals.jbchem.a130973

keywords:

subject

Has Abstract

pub_date

1975-10-01 00:00:00

pages

825-34

issue

4

eissn

0021-924X

issn

1756-2651

journal_volume

78

pub_type

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