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Journal of Lipid Research, Vol. 13, 477-482, July 1972
Copyright © 1972 by Lipid Research, Inc.
Department of Biochemistry, Faculty of Sciences, Mahidol University, Rama VI Road, Bangkok, Thailand
Carotene 15,15'-dioxygenase, which oxidizes carotenoids to retinal, has been purified up to 200-fold from rabbit intestine by ammonium sulfate fractionation, heat treatment, and acetone precipitation. With ßbeta;-apo-10'-carotenol as the substrate, the purified enzyme has a pH optimum of 7.8, a Km of 6.7 x 10-5 m, and a Vmax at 37°C of 9 nmoles of retinal/mg protein/hr. The purified enzyme is inhibited by ferrous ion-chelating agents such as 
,'-dipyridyl and o-phenanthroline, and by sulfhydryl-binding agents such as iodoacetamide, N-ethylmaleimide, and p-chloromercuribenzoate. The latter inhibitory effects are reversed by reduced glutathione. The cleavage of ßbeta;-apo-10'-carotenol is competitively inhibited by its acetylenic analog, 15,15'-dehydro-ßbeta;-apo-10'-carotenol. The enzyme is present in the intestinal mucosa of several mammals, the chicken, the tortoise, and a freshwater fish, but it is absent from cat intestinal tissue.
Supplementary key words ßbeta;-apo-10'-carotenol • ßbeta;-carotene cleavage • 15,15'-dehydro-ßbeta;-apo-10'-carotenol • retinal • thiobarbituric acid method • mammals • fish • tortoise • chicken • cat
Submitted on October 4, 1971
Accepted on March 29, 1972
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