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PMID: 6213615 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

The specificity of carboxyl group modification during the inactivation of the Escherichia coli F1-ATPase with dicyclohexyl[14C]carbodiimide.

The Journal of biological chemistry ·Vol. 257 ·No. 17 ·1982-09-10 ·Pages 10033-7

Yoshida M, Allison WS, Esch FS, Futai M

Abstract

暂无摘要

MeSH Terms

Adenosine Triphosphatases/antagonists & inhibitors Amino Acid Sequence Amino Acids/analysis Carbodiimides/pharmacology Carbon Radioisotopes Cyanogen Bromide Dicyclohexylcarbodiimide/pharmacology Escherichia coli/enzymology Membrane Proteins/antagonists & inhibitors Peptide Fragments/isolation & purification Proton-Translocating ATPases Trypsin

Chemicals

Amino Acids Carbodiimides Carbon Radioisotopes Membrane Proteins Peptide Fragments Dicyclohexylcarbodiimide Trypsin Adenosine Triphosphatases Proton-Translocating ATPases Cyanogen Bromide

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Yoshida M

Allison W S

Esch F S

Futai M

Article Info

Journal

The Journal of biological chemistry

Abbr.

J Biol Chem

ISSN

0021-9258

Published

1982-09-10

Pages

10033-7

Language

English

Region

United States

NLM ID

2985121R

Subset

Grants

NIGMS NIH HHS · GM-16974 · United States

External Links

PubMed source View journal details

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The specificity of carboxyl group modification during the inactivation of the Escherichia coli F1-ATPase with dicyclohexyl[14C]carbodiimide.

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