Interaction of cytochrome c with the phosphorprotein phosvitin.
Candida krusei cytochrome c forms a molecular complex with phosphorprotein phosvitin in weakly alkaline solution of low ionic strength. At most, about 22 molecules of cytochrome c bind to a phosvitin molecule. The complex at the binding ratio below about 11 (half of the maximum ratio) as a much higher binding strength. Several lines of evidence indicate that the marked difference in the binding strength is due to the difference in negative charges on phosvitin molecule concerned in the binding of a cytochrome c molecule. The phosvitin-bound cytochrome c seems to have a preferred orientation with the front surface of the molecule containing the exposed heme edge in contact with the phosvitin molecule.
D000818:Animals; D002175:Candida; D003574:Cytochrome c Group; D004527:Egg Proteins; D006736:Horses; D007700:Kinetics; D008970:Molecular Weight; D009206:Myocardium; D010774:Phosvitin; D011485:Protein Binding; D011487:Protein Conformation; D013045:Species Specificity; D013050:Spectrometry, Fluorescence
D003574:Cytochrome c Group; D004527:Egg Proteins; D010774:Phosvitin