Publication: Purification and properties of carotene 15,15' dioxygenase of rabbit intestine
Issued Date
1972-12-01
Resource Type
ISSN
00222275
Other identifier(s)
2-s2.0-0015480054
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Mahidol University
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SCOPUS
Bibliographic Citation
Journal of Lipid Research. Vol.13, No.4 (1972), 477-482
Suggested Citation
M. R. Lakshmanan, H. Chansang, J. A. Olson Purification and properties of carotene 15,15' dioxygenase of rabbit intestine. Journal of Lipid Research. Vol.13, No.4 (1972), 477-482. Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/9996
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Title
Purification and properties of carotene 15,15' dioxygenase of rabbit intestine
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Abstract
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 β apo 10' carotenol as the substrate, the purified enzyme has a pH optimum of 7.8, a K(m) of 6.7 x 10 -5 M, and a V(max) at 37° C of 9 nmoles of retinal/mg protein/hr. The purified enzyme is inhibited by ferrous ion chelating agents such as α,α' 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 β apo 10' carotenol is competitively inhibited by its acetylenic analog, 15,15' dehydro β 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.