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PMID: 1238117 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Purine and pyrimidine inhibitors of arginase.

Biochimica et biophysica acta ·Vol. 410 ·No. 1 ·1975-11-20 ·Pages 164-6

Rosenfeld JL, Dutta SP, Chheda GB, Tritsch GL

Abstract

1. Adenosine, inosine, adenine and uric acid are competitive inhibitors and cytidine and cytosine noncompetitive inhibitors of bovine liver arginase (L-arginine amidinohydrolase, EC 3.5.3.1). 2. The affinity of the enzyme for these inhibitors was 10--100 times as great as for substrate in terms of Ki versus Km. 3. These nucleic acid metabolites may thus function in vivo to regulate the urea cycle. 4. Several naturally occuring competitive and noncompetitive inhibitors of arginase of unknown structure have been isolated from plant and animal tissue. From their properties and methods of isolation, they may be the purines and pyrimidines herein described. 5. These purines and pyrimidines have no effect on tryptic hydrolysis.

MeSH Terms
Animals Arginase/antagonists & inhibitors Binding, Competitive Cattle Kinetics Liver/enzymology Purines/pharmacology Pyrimidines/pharmacology Structure-Activity Relationship
Chemicals
Purines Pyrimidines Arginase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Rosenfeld J L
Dutta S P
Chheda G B
Tritsch G L
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1975-11-20
Pages
164-6
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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