| Literature DB >> 213363 |
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.Entities:
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Year: 1978 PMID: 213363 DOI: 10.1515/bchm2.1978.359.2.1005
Source DB: PubMed Journal: Hoppe Seylers Z Physiol Chem ISSN: 0018-4888