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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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|
|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|
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