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PMID: 6114709 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Evidence that regulation of hepatic guanylate cyclase activity involves interactions between catalytic site -SH groups and both substrate and activator.

Archives of biochemistry and biophysics ·Vol. 208 ·No. 1 ·1981-04-15 ·Pages 75-86

Ignarro LJ, Kadowitz PJ, Baricos WH

Abstract

暂无摘要

MeSH Terms

Animals Binding Sites/drug effects Catalysis Chromatography, Gel Enzyme Activation/drug effects Guanylate Cyclase/antagonists & inhibitors,metabolism Liver/enzymology Male Nitroso Compounds/pharmacology Oxidation-Reduction/drug effects Rats Substrate Specificity Sulfhydryl Compounds/pharmacology

Chemicals

Nitroso Compounds Sulfhydryl Compounds Guanylate Cyclase

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Ignarro L J

Kadowitz P J

Baricos W H

Article Info

Journal

Archives of biochemistry and biophysics

Abbr.

Arch Biochem Biophys

ISSN

0003-9861

DOI

10.1016/0003-9861(81)90125-9

Published

1981-04-15

Pages

75-86

Language

English

Region

United States

NLM ID

0372430

Subset

Grants

NIADDK NIH HHS · 1-KO4 AM 00076 · United States

NIADDK NIH HHS · AM 17692 · United States

NHLBI NIH HHS · HL 18070 · United States

External Links

PubMed source DOI: 10.1016/0003-9861(81)90125-9 View journal details

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Evidence that regulation of hepatic guanylate cyclase activity involves interactions between catalytic site -SH groups and both substrate and activator.

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