Purification and characterization of corn glutathione S-transferase.

Abstract:

:Two glutathione S-transferase (GST) activities have been identified and purified from etiolated corn tissue. The first, designated GST I enzyme, is constitutively present in corn tissue, and the second, designated GST II enzyme, is present only in tissue which has been treated with chemical antidotes which protect corn against chloroacetanilide herbicides. The total activity constitutes approximately 2% of the soluble protein in these tissues. The native forms of these enzymes have molecular weights of approximately 50 000 as determined by Sephadex G-100 chromatography. On sodium dodecyl sulfate-polyacrylamide gels, GST I enzyme migrates primarily as a single band of molecular weight 29 000, and GST II enzyme migrates as primarily two bands of molecular weight 29 000 and 27 000. Both enzymes catalyze the formation of a glutathione-herbicide conjugate in vitro when the herbicide alachlor is used as a substrate. This conjugation results in elimination of the biological activity of the herbicide.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Mozer TJ,Tiemeier DC,Jaworski EG

doi

10.1021/bi00274a011

subject

Has Abstract

pub_date

1983-03-01 00:00:00

pages

1068-72

issue

5

eissn

0006-2960

issn

1520-4995

journal_volume

22

pub_type

杂志文章