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J. Biochem, 1968, Vol. 63, No. 2 242-248
© 1968 Japanese Biochemical Society

research-article

The Factor Activating Protoheme Ferro-lyase in Chicken Hemolysate Supernatant*

I. Some Properties of the Cofactor

TOSHIO ASAKURA**, ATSUSHI TAKAGI, SHIGEKI MINAKAMI, YOSHIMASA YONEYAMA*** and HARUHISA YOSHIKAWA

From the Department of Physiological Chemistry and Nutrition, Faculty of Medicine, University of Tokyo Bunkyo-ku, Tokyo

** Present address: The School of Medicine, Johnson Research Foundation, University of Pennsylvania, Philadelphia, U.S.A.

*** Present address: Department of Biochemistry, Faculty of Medicine, University of Kanazawa, Kanazawa.

A fraction of the supernatant of a chicken hemolysate was shown to contain some cofactor which accelerated heme synthesis catalyzed by protoheme ferro-lyase [EC 4.99.1.1 [EC] ]. The supernatant fraction itself had no enzyme activity. The cofactor was heat labile and non-dialyzable. Results indicated that the cofactor was not globin as previously supposed and also that it was not acting as a reducing agent. The cofactor was found to precipitate on storage in a refrigerator for more than two weeks.

Protoporphyrin, the substrate of the reaction could not be replaced by the protoporphyrin-globin complex. The mechanism of heme formation is discussed.

*Dedicated to Dr. Koozoo Kaziro, Professor Emeritus of the Nippon Medical School, on the occasion of his 70th birthday.


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