Document Detail


Studies on cytochrome c oxidase, IX. The primary structure of polypeptide VIa.
MedLine Citation:
PMID:  6292069     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The complete amino acid sequence of the cytoplasmic polypeptide VIa of cytochrome c oxidase from beef heart is described. The primary structure of this component of complex IV of the respiratory chain is elucidated by isolation and sequencing of overlapping glutamic acid, arginine, tryptophan and methionine fragments obtained by cleavage with Staphylococcus aureus protease, protease from submaxillaris glands of mice, 2-iodosylbenzoic acid and cyanogen bromide. The chain length of polypeptide VIa is 98 amino acids, the resulting molecular mass of 10670 Da. The hydrophilic protein does not contain a hydrophobic membrane penetrating sequence domain. Its function in the respiratory complex IV is unknown.
Authors:
R Biewald; G Buse
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Hoppe-Seyler's Zeitschrift für physiologische Chemie     Volume:  363     ISSN:  0018-4888     ISO Abbreviation:  Hoppe-Seyler's Z. Physiol. Chem.     Publication Date:  1982 Oct 
Date Detail:
Created Date:  1983-01-19     Completed Date:  1983-01-19     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  2985060R     Medline TA:  Hoppe Seylers Z Physiol Chem     Country:  GERMANY, WEST    
Other Details:
Languages:  eng     Pagination:  1141-53     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Amino Acids / analysis
Animals
Cattle
Chemical Phenomena
Chemistry
Chromatography, Gel
Cyanogen Bromide
Electron Transport Complex IV*
Myocardium / enzymology
Peptide Fragments*
Peptide Hydrolases
Submandibular Gland / enzymology
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Peptide Fragments; 506-68-3/Cyanogen Bromide; EC 1.9.3.1/Electron Transport Complex IV; EC 3.4.-/Peptide Hydrolases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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