Effect of uridine diphospho-N-acetylglucosamine and sodium salicylate on L-glutamine-D-fructose-6-phosphate aminotransferase activity from rat gastric mucosa.

Abstract:

:Mechanisms of inhibitory action of sodium salicylate on L-glutamine-D-fructose-6-phosphate aminotransferase, prepared from rat gastric mucosa, were studied. Sodium salicylate at lower concentrations (10-20 mM) inhibited reversibly aminotransferase activity by competing with fructose-6-phosphate. At higher concentrations, sodium salicylate inactivated the enzyme irreversibly, with an inactivation rate following first-order kinetics with respect to the enzyme concentration. Uridine-5'-diphospho-N-acetylglucosamine is an endogenous feedback inhibitor. It inhibited the aminotransferase-catalyzed reaction also by competing with fructose-6-phosphate but with an inhibiting activity 1000 times that of sodium salicylate. Uridine-5'-diphospho-N-acetylglucosamine reduced the salicylate inhibition of the enzymic reaction and protected the enzyme from salicylate-induced irreversible inactivation. At a fixed concentration of uridine-5'-diphospho-N-acetylglucosamine (7x10(-6)M), an increase of salicylate concentration produced an increase in enzyme activity as compared with the control.

journal_name

J Pharm Sci

authors

Chan J,Lee KH

doi

10.1002/jps.2600640711

subject

Has Abstract

pub_date

1975-07-01 00:00:00

pages

1182-5

issue

7

eissn

0022-3549

issn

1520-6017

pii

S0022-3549(15)40292-8

journal_volume

64

pub_type

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