Ustilago cytochrome

The hydrodynamic properties of Ustilago cytochrome c were investigated by Thelander (86). He found the partial specific volume to be 0.721 ml/g and the molecular weight, by sedimentation equilibrium, to be 15,500. The latter value, although higher than that given by summation of the constituent amino acid residues (i.e., 11,877, see Table 3), indicates that the protein is monomeric. 

The data presented in Table 3, which includes the amino acid composition of baker s yeast and Candida krusei cytochrome c for comparison, show that Ustilago and Neurospora cytochrome c contain the same number of total residues. In seven instances, the number of residues of a particular amino acid/mole are identical. Thus, even in the absence of a sequence for the Ustilago cytochrome it can be concluded that this protein, unlike the siderochromes, has suffered little alteration in the progression from the Ascomycetes to the Basidiomycetes. This can be ascribed to the varying function of the two types of molecules. Cytochrome c must fit into a relatively specific slot bounded by a reductase and an oxidase and it has hence evolved much more slowly than the more freely acting transport agents where the specificity constraints are less demanding. 

According to Komai (85) crystalline Ustilago cytochrome c isolated by cell fracture rather than by alkaline extraction also displays a neutral isoelectric point. 

Acknowledgment. The author is indebted to A. Baldesten for performing amino acid analyses on Ustilago cytochrome c. 

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