JBC, Vol. 253, Issue 12, 4402-4407, Jun, 1978
Identification of enzymically inactive apocytochrome c peroxidase in anaerobically grown Saccharomyces cerevisiae
L. Djavadi-Ohaniance, Y. Rudin and G. Schatz
Anaerobically grown yeast cells lack cytochrome c peroxidase activity but
rapidly acquire it upon aeration. In order to study the oxygen-induced
formation of this hemoprotein, extracts of anaerobic and aerobic yeast
cells were resolved by one- and two-dimensional acrylamide gel
electrophoresis and the separated polypeptides were then checked for
comigration with radiolabeled purified cytochrome c peroxidase from aerobic
cells or for reaction with cytochrome c peroxidase antiserum. Both types of
extracts contained roughly equal amounts of a polypeptide which was
indistinguishable from apocytochrome c peroxidase with respect to
antigenicity, isoelectric point, and apparent molecular weight in three
different gel systems. In confirmation of an earlier report by Sels. A.A.,
and Cocriamont, C. (1968) (Biochem. Biophus. Res. Commun. 32, 192-198) the
oxygen-induced formation of cytochrome c peroxidase was insensitive to
inhibitors of protein synthesis and could be mimicked by the addition of
heme to extracts of anaerobic cells. We conclude that the oxygen-induced
formation of yeast cytochrome c peroxidase involves the addition of heme to
the apoenzyme which is already present in the anaerobically grown cells.
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