| Autor: |
Ludwig, Bernd, Suda, Kitaru, Cerletti, Nico |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 12/15/83, Vol. 137 Issue 3, p597-602, 6p |
| Abstrakt: |
Cytochrome c1 was purified from the bacterium Paracoccus denitrificans. It is an acidic, hydrophobic polypeptide with an apparent molecular weight of around 65000 and a single, covalently attached home; it cross-reacts immunologically with cytochrome c1 from yeast mitochondria. The amino acid sequence of the tryptic heme peptide of the bacterial cytochrome c1 shows extensive homology to the corresponding region of beef heart cytochrome C1 [Wakabayashi S. et al. (1982) J. Biol Chem. 257, 9335–9344]. Positive evidence for a stable association of the Paracoccus cytochrome c1 with other polypeptides and b-type heme components (‘bc1-complex’) has not yet been obtained. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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