| Literature DB >> 2546794 |
M Rönnberg1, N Kalkkinen, N Ellfolk.
Abstract
The primary structure of Pseudomonas cytochrome c peroxidase is presented. The intact protein was fragmented with cyanogen bromide into five fragments; partial cleavage was observed at a Met-His bond of the protein. The primary structure was established partly by automatic Edman degradations, partly by manual sequencing of peptides obtained with trypsin, thermolysin, chymotrypsin, pepsin, subtilisin and Staphylococcus aureus V8 endopeptidase. The order of the cyanogen bromide fragments was further confirmed by overlapping peptides obtained by specific cleavage of the whole protein. Pseudomonas cytochrome c peroxidase consists of 302 amino acid residues giving a calculated Mr of 33690.Entities:
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Year: 1989 PMID: 2546794 DOI: 10.1016/0014-5793(89)80714-8
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124