Literature DB >> 2988583

Studies on cytochrome c oxidase, XI. The amino-acid sequence of bovine heart polypeptide VIc.

M Erdweg, G Buse.   

Abstract

The complete primary structure of the cytoplasmically synthesized polypeptide VIc from beef heart cytochrome c oxidase was determined via isolation and sequencing of overlapping methionine and glutamic acid fragments. The protein consists of 73 amino acids (Mr 8 480). Through the protein contains, from residues 21 to 40, a hydrophobic sequence interrupted by one lysine it may not penetrate the membrane. A sequence of 33 amino acids highly homologous to the C-terminal part of VIc has been translated from a cDNA clone of a nuclear coded subunit of the enzyme from rat liver. The function of this component of the terminal oxidase is yet unknown.

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Year:  1985        PMID: 2988583     DOI: 10.1515/bchm3.1985.366.1.257

Source DB:  PubMed          Journal:  Biol Chem Hoppe Seyler        ISSN: 0177-3593


  3 in total

1.  The transmembrane helices of beef heart cytochrome oxidase.

Authors:  M Lundeen; B Chance; L Powers
Journal:  Biophys J       Date:  1987-04       Impact factor: 4.033

2.  Nucleotide sequence of cDNA encoding human cytochrome c oxidase subunit VIc.

Authors:  M Otsuka; Y Mizuno; M Yoshida; Y Kagawa; S Ohta
Journal:  Nucleic Acids Res       Date:  1988-11-25       Impact factor: 16.971

3.  Tissue-specific regulation of bovine heart cytochrome-c oxidase activity by ADP via interaction with subunit VIa.

Authors:  G Anthony; A Reimann; B Kadenbach
Journal:  Proc Natl Acad Sci U S A       Date:  1993-03-01       Impact factor: 11.205

  3 in total

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