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Glutathione S-transferase isozymes of mouse intestine: differential induction by 2(3)-tert-butyl-4-hydroxyanisole.

Abstract：

:Electrofocusing of mouse small intestine mucosal cytosol yielded two prominent peaks of glutathione S-transferase activity, at pH 8.7 and pH 9.0. These intestinal transferases were indistinguishable from corresponding liver transferases in immunological reactivities and in several other properties. Dietary t-butyl-4-hydroxyanisole increased intestine cytosol protein immunologically identical to the liver transferase with pI of 8.7 and also elevated markedly and preferentially the intestinal transferase activity peak at pH 8.7. Thus, the predominant transferases of mouse intestine appear identical to two of the liver isozymes, and t-butyl-4-hydroxyanisole enhances intestinal transferase activity mainly by increasing the quantity of the isozyme(s) of pI 8.7.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Parchment RE,Benson AM

doi

10.1016/0006-291x(84)90875-1

subject

Has Abstract

pub_date

1984-03-30 00:00:00

pages

1015-21

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(84)90875-1

journal_volume

119

pub_type

杂志文章

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