Studies on the two phosphoenzyme conformations of Na+ plus K+-ATPase.

Annals of the New York Academy of Sciences ·Vol. 242 ·1974-00-00 ·Pages 120-32

Tobin T, Akera T, Brody TM

Abstract

暂无摘要

MeSH Terms

Adenosine Triphosphatases/metabolism Adenosine Triphosphate/analogs & derivatives,pharmacology Animals Binding Sites Brain/enzymology Calcium/pharmacology Chelating Agents/pharmacology Edetic Acid/pharmacology Enzyme Activation/drug effects Guinea Pigs Kinetics Ligands Magnesium/pharmacology Ouabain/pharmacology Phosphates/pharmacology Phosphoproteins/metabolism Potassium/pharmacology Protein Binding Protein Conformation Rats Sodium/pharmacology Time Factors Tritium

Chemicals

Chelating Agents Ligands Phosphates Phosphoproteins Tritium Ouabain Adenosine Triphosphate Edetic Acid Sodium Adenosine Triphosphatases Magnesium Potassium Calcium

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Tobin T

Akera T

Brody T M

Article Info

Journal

Annals of the New York Academy of Sciences

Abbr.

Ann N Y Acad Sci

ISSN

0077-8923

DOI

10.1111/j.1749-6632.1974.tb19084.x

Published

1974-00-00

Pages

120-32

Language

English

Region

United States

NLM ID

7506858

Subset

External Links

PubMed source DOI: 10.1111/j.1749-6632.1974.tb19084.x View journal details

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Studies on the two phosphoenzyme conformations of Na+ plus K+-ATPase.

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