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PMID: 203583 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Differentiation of nucleotide binding sites and role of metal ion in the adenylate kinase reaction by 31P NMR. Equilibria, interconversion rates, and NMR parameters of bound substrates.

The Journal of biological chemistry ·Vol. 253 ·No. 4 ·1978-02-25 ·Pages 1149-58

Nageswara Rao BD, Cohn M, Noda L

Abstract

暂无摘要

MeSH Terms

Adenosine Diphosphate Adenosine Triphosphate Adenylate Kinase/metabolism Animals Binding Sites Fishes Kinetics Magnesium/pharmacology Magnetic Resonance Spectroscopy Mathematics Muscles/enzymology Phosphotransferases/metabolism Protein Binding Protein Conformation Swine

Chemicals

Adenosine Diphosphate Adenosine Triphosphate Phosphotransferases Adenylate Kinase Magnesium

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Nageswara Rao B D

Cohn M

Noda L

Article Info

Journal

The Journal of biological chemistry

Abbr.

J Biol Chem

ISSN

0021-9258

Published

1978-02-25

Pages

1149-58

Language

English

Region

United States

NLM ID

2985121R

Subset

External Links

PubMed source View journal details

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Differentiation of nucleotide binding sites and role of metal ion in the adenylate kinase reaction by 31P NMR. Equilibria, interconversion rates, and NMR parameters of bound substrates.

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