Purification and some properties of glutathione-S-epoxide transferase from guinea pig liver.

Abstract:

:Glutathione-S-epoxide transferase has been purified from guinea pig liver in a homogeneous form having a sedimentation coefficient, s20,w of 3.8S, and a molecular weight of 46,000, and dissociable into subunits with a molecular weight of 25,000. The activities with four substrates, styrene oxide, naphthalene oxide, iodomethane, and p-nitrobenzyl chloride, were all copurified during purification of the enzyme from 100,000 X g supernatant of guinea pig liver. However, kinetic data suggest different mechanisms for the glutathione conjugating reaction with iodomethane and p-nitrobenzyl chloride. The view that the epoxide transferase does not distinguish between simple epoxides and arene oxides has been confirmed with the guinea pig liver enzyme.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Hayakawa T,Myokei Y,Yagi H,Jerina DM

subject

Has Abstract

pub_date

1977-08-01 00:00:00

pages

407-15

issue

2

eissn

0021-924X

issn

1756-2651

journal_volume

82

pub_type

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