Subunit composition, function, and spatial arrangement in the Ca2+-and Mg2+-activated adenosine triphosphatases of Escherichia coli and Salmonella typhimurium.

Archives of biochemistry and biophysics ·Vol. 167 ·No. 1 ·1975-03-00 ·Pages 311-21

Bragg PD, Hou C

Abstract

暂无摘要

MeSH Terms

Adenosine Triphosphatases/metabolism Calcium/pharmacology Disulfides Electrophoresis, Polyacrylamide Gel Enzyme Activation/drug effects Escherichia coli/enzymology Macromolecular Substances Magnesium/pharmacology Molecular Weight Propionates Protein Binding Protein Conformation Salmonella typhimurium/enzymology Species Specificity Succinimides Trypsin

Chemicals

Disulfides Macromolecular Substances Propionates Succinimides Trypsin Adenosine Triphosphatases Magnesium Calcium

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Bragg P D

Hou C

Article Info

Journal

Archives of biochemistry and biophysics

Abbr.

Arch Biochem Biophys

ISSN

0003-9861

DOI

10.1016/0003-9861(75)90467-1

Published

1975-03-00

Pages

311-21

Language

English

Region

United States

NLM ID

0372430

Subset

External Links

PubMed source DOI: 10.1016/0003-9861(75)90467-1 View journal details

Analysis Services

Subunit composition, function, and spatial arrangement in the Ca2+-and Mg2+-activated adenosine triphosphatases of Escherichia coli and Salmonella typhimurium.

Contact

WeChat Official Account