Studies on the biosynthesis of cytochrome P-450 in rat liver—A probe with phenobarbital

Bhat, Kolari S and Padmanaban, Govindarajan (1979) Studies on the biosynthesis of cytochrome P-450 in rat liver—A probe with phenobarbital. In: Archives of Biochemistry and Biophysics , 198 (1). pp. 110-116.

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Abstract

Cytochrome P-450 has been purified from phenobarbital-treated rat livers to a specific content of 17 nmol/mg protein. The major species purified has a molecular weight of 48,000. Using the purified antibody for the cytochrome P-450 preparation it has been shown that the major product synthesized in vivo and in the homologous cell-free system in vitro is the 48,000 molecular weight species. Poly(A)-containing RNA isolated from phenobarbital-treated animals codes for the synthesis of the 48,000 molecular weight species in the wheat germ and reticulocyte lysate cell-free systems. It is concluded that cytochrome P-450 synthesis does not involve processing of a polyprotein precursor, although certain minor modifications including glycosylation of the primary translation product are not ruled out. Phenobarbital treatment of the animal results in a significant increase in the cytochrome P-450 messenger activity as measured in the wheat germ cell-free system.

Item Type:	Journal Article
Publication:	Archives of Biochemistry and Biophysics
Publisher:	Elsevier Science
Additional Information:	Copyright of this article belongs to Elsevier Science.
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	27 Dec 2010 13:08
Last Modified:	27 Dec 2010 13:08
URI:	http://eprints.iisc.ac.in/id/eprint/33902

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