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PMID: 6213230 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The DCCD-binding polypeptide is close to the F1 ATPase-binding site on the cytoplasmic surface of the cell membrane of Escherichia coli.

Biochemical and biophysical research communications ·Vol. 106 ·No. 2 ·1982-05-31 ·Pages 400-6

Loo TW, Bragg PD

Abstract

暂无摘要

MeSH Terms

Adenosine Triphosphatases/metabolism Antigen-Antibody Complex Carrier Proteins/metabolism Cell Membrane/metabolism Dicyclohexylcarbodiimide/pharmacology Escherichia coli/metabolism Immune Sera Kinetics Membrane Proteins/metabolism Proton-Translocating ATPases

Chemicals

Antigen-Antibody Complex Carrier Proteins Immune Sera Membrane Proteins Dicyclohexylcarbodiimide Adenosine Triphosphatases Proton-Translocating ATPases

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Loo T W

Bragg P D

Article Info

Journal

Biochemical and biophysical research communications

Abbr.

Biochem Biophys Res Commun

ISSN

0006-291X

DOI

10.1016/0006-291x(82)91124-x

Published

1982-05-31

Pages

400-6

Language

English

Region

United States

NLM ID

0372516

Subset

External Links

PubMed source DOI: 10.1016/0006-291x(82)91124-x View journal details

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The DCCD-binding polypeptide is close to the F1 ATPase-binding site on the cytoplasmic surface of the cell membrane of Escherichia coli.

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