title: The primary structure of Pseudomonas cytochrome c peroxidase.
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.
authors.affiliation: Department of Biochemistry, University of Helsinki, Finland.
authors.forename: M
authors.initials: M
authors.lastname: Rönnberg
authors.forename: N
authors.initials: N
authors.lastname: Kalkkinen
authors.forename: N
authors.initials: N
authors.lastname: Ellfolk
mesh_terms: D000595:Amino Acid Sequence; D003578:Cytochrome-c Peroxidase / Q000378:metabolism*; D008969:Molecular Sequence Data; D010544:Peroxidases / Q000378:metabolism*; D011487:Protein Conformation; D011549:Pseudomonas / Q000201:enzymology*
chemical_list: D010544:Peroxidases; D003578:Cytochrome-c Peroxidase