par Polastro, Enrico 
;Looze, Yvan ;Leonis, José
Référence Phytochemistry, 16, 6, page (639-641)
Publication Publié, 1977
;Looze, Yvan ;Leonis, José Référence Phytochemistry, 16, 6, page (639-641)
Publication Publié, 1977
Article révisé par les pairs
| Résumé : | The Km and Vmax values characterizing the reaction of baker's yeast iso-I-cytochrome c, whether tri-methylated or not at lysine residue 72, with crude preparations of cytochrome c peroxidase, cytochrome c oxidase and succinate cytochrome c oxidoreductase from Saccharomyces cerevisiae are similar. These results, as well as the redox potential values, the auto-oxidability parameters and the circular dichroism spectra, strongly suggest that the biological methylation of yeast cytochrome c does not alter its functional properties. The functional characteristics of baker's yeast iso-I-cytochrome c are similar to those of horse heart cytochrome c and yeast iso-2-cytochrome c. © 1977. |
