Home LiteratureArticle Details
PMID: 143953 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Characterization of the purified membrane attachment (beta) subunit of the proton translocating adenosine triphosphatase from Escherichia coli.

Biochemistry ·Vol. 16 ·No. 18 ·1977-09-06 ·Pages 4020-5

Sternweis PC, Smith JB

Abstract

暂无摘要

MeSH Terms
Adenosine Triphosphatases/analysis,metabolism Amino Acids/analysis Bacterial Proteins/metabolism Biological Transport, Active Escherichia coli/enzymology Membrane Proteins/metabolism Molecular Weight Oxidative Phosphorylation Peptides/isolation & purification Protein Binding Protein Conformation Protons Spectrum Analysis
Chemicals
Amino Acids Bacterial Proteins Membrane Proteins Peptides Protons Adenosine Triphosphatases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Sternweis P C
Smith J B
Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
0006-2960
Published
1977-09-06
Pages
4020-5
Language
English
Region
United States
NLM ID
0370623
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com