Cytochrome c peroxidase compound I: formation of covalent protein crosslinks during the endogenous reduction of the active site.
Biochim Biophys Acta
; 872(1-2): 155-7, 1986 Jul 25.
Article
em En
| MEDLINE
| ID: mdl-3015215
ABSTRACT
Cytochrome c peroxidase (ferrocytochrome-chydrogen-peroxide oxidoreductase, EC 1.11.1.5) was oxidized by hydrogen peroxide in the absence of exogenous electron donor. Higher molecular weight species were observed in the decay products at pH 4.5. Monomer and dimer were separated by gel filtration and purified by anion-exchange chromatography. Peptide mapping of tryptic digests of the dimer indicated a tyrosine crosslink localized between residues 32 and 48 of the native enzyme.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peroxidases
/
Citocromo-c Peroxidase
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1986
Tipo de documento:
Article