Studies on Cytochrome-c Oxidase, XIII. Amino-Acid Sequence of the Small Membrane Polypeptide VIIIc from Bovine Heart Respiratory Complex IV
- 1 January 1986
- journal article
- research article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 367 (1) , 67-74
- https://doi.org/10.1515/bchm3.1986.367.1.67
Abstract
The isolation and complete amino-acid sequence analysis of the cytoplasmically synthesized polypeptide VIIIc from bovine heart cytochrome-c oxidase is described. The protein is a stoichiometric constituent of the mitochondrial respiratory complex IV. Its primary structure is deduced from N-terminal sequencing and peptides obtained by enzymatic cleavage with Staphylococcus aureus proteinase and chemical cleavage with cyanogen bromide. The small protein consists of 56 amino acids summing up to a total Mr of 6243. From position 34 to 51 the chain contains a hydrophobic sequence of 18 residues. This probable membrane-spanning segment also contains the 2 cysteine residues of the chain. The function of this subunit in the respiratory complex IV is still unknown.This publication has 16 references indexed in Scilit:
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