Abstract
n-Octylamine binds to oxidized liver microsomal cytochrome P-450 to produce a difference spectrum similar to type II binding. This binding spectrum has been used to determine the relative amounts of two forms of cytochrome P-450 in rabbit and mouse microsomes. These two forms of the hemeprotein have been proposed by others to be high- and low-spin cytochrome P-45O, and pretreatment of rabbits and mice with 3-methylcholanthrene results in a change in the ratio of these two forms of the hemeprotein. In contrast to these earlier studies, pretreatment of rats with 3-methylcholanthrene results in no significant change in the ratio of these two forms of the hemeprotein, which indicates a marked species difference. These studies demonstrate that the n-octylamine binding method is not a criterion of induction of the 3-methylcholanthrene-induced hemeprotein in the rat.
Footnotes
- Received November 20, 1972.
- Copyright © 1973 by The American Society for Pharmacology and Experimental Therapeutics
DMD articles become freely available 12 months after publication, and remain freely available for 5 years.Non-open access articles that fall outside this five year window are available only to institutional subscribers and current ASPET members, or through the article purchase feature at the bottom of the page.
|