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PMID: 213363 Published · ppublish English Journal Article

Studies on cytochrome c oxidase, II. The chemical constitution of a short polypeptide from the beef heart enzyme.

Hoppe-Seyler's Zeitschrift fur physiologische Chemie ·Vol. 359 ·No. 8 ·1978-08-00 ·Pages 1005-9

Buse G, Steffens GJ

Abstract

A low molecular weight (approximately 6000) polypeptide fraction was isolated from beef heart cytochrome c oxidase, consisting of three peptides with the N-terminal end groups isoleucine, phenylalanine and serine. The complete amino acid sequence of the serine component is described. From the chemical constitution, a site-specific cleavage from a precursor protein and a possible function in membrane penetration and complex formation of the oxidase is inferred.

MeSH Terms
Amino Acid Sequence Amino Acids/analysis Animals Cattle Chromatography, Gel Cytochrome c Group Electron Transport Complex IV/analysis In Vitro Techniques Molecular Weight Myocardium/enzymology Peptide Fragments/isolation & purification Protein Conformation
Chemicals
Amino Acids Cytochrome c Group Peptide Fragments Electron Transport Complex IV
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Buse G
Steffens G J
Article Info
Journal
Hoppe-Seyler's Zeitschrift fur physiologische Chemie
Abbr.
Hoppe Seylers Z Physiol Chem
ISSN
0018-4888
Published
1978-08-00
Pages
1005-9
Language
English
Region
Germany
NLM ID
2985060R
Subset
IM
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