The primary structure of Pseudomonas cytochrome c peroxidase.

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Citation

Ronnberg M, Kalkkinen N, Ellfolk N

The primary structure of Pseudomonas cytochrome c peroxidase.

FEBS Lett. 1989 Jul 3;250(2):175-8.

PubMed ID
2546794 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Cytochrome c551 peroxidaseP14532Details