Chemical modification of rat liver arginase.

Abstract:

:Chemical modifications were used to search for catalytically important residues of rat liver arginase. The results of carbamoylation, nitration and diazotization suggest that lysyl and tyrosyl residues are not involved in the catalytic function of arginase. The modification of 5--6 tryptophanyl residues by N-bromosuccinimide or 2-hydroxy-5-nitrobenzyl bromide led to about 90% inhibition of the enzyme activity. Photooxidation of 21 histydyl residues also led to considerable inactivation of arginase. The modification of tryptophanyl and histidyl residues did not cause dissociation of the enzyme into subunits.

journal_name

Acta Biochim Pol

journal_title

Acta biochimica Polonica

authors

Ber E,Muszyńska G

subject

Has Abstract

pub_date

1979-01-01 00:00:00

pages

103-14

issue

1-2

eissn

0001-527X

issn

1734-154X

journal_volume

26

pub_type

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