The primary structure ofPseudomonascytochromecperoxidase
| Autor: | Nils Ellfolk, Marjaana Rönnberg, Nisse Kalkkinen |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
Cytochrome
Protein Conformation Molecular Sequence Data Primary structure Biophysics Biochemistry (Pseudomonas aeruginosa) 03 medical and health sciences chemistry.chemical_compound Structural Biology Thermolysin Pseudomonas Genetics medicine Amino Acid Sequence Molecular Biology 030304 developmental biology 0303 health sciences Chymotrypsin biology Chemistry Cytochrome c peroxidase Heme-binding site 030302 biochemistry & molecular biology Protein primary structure Subtilisin Cell Biology Trypsin 3. Good health Peroxidases biology.protein Cytochrome-c peroxidase Cyanogen bromide medicine.drug |
| Zdroj: | FEBS Letters. 250:175-178 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(89)80714-8 |
| Popis: | 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 M r of 33 690. |
| Databáze: | OpenAIRE |
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