Membrane bound cytochrome p-450 determines the optimal temperatures of NADPH - cytochrome p-450 reductase and cytochrome p-450-linked monooxygenase reactions in rat and trout hepatic microsomes

Prema , Gurumurthy and Mannering, Gilbert J (1985) Membrane bound cytochrome p-450 determines the optimal temperatures of NADPH - cytochrome p-450 reductase and cytochrome p-450-linked monooxygenase reactions in rat and trout hepatic microsomes. Biochemical and Biophysical research communications, 127 (2). pp. 571-577. ISSN Print: 0006-291X Online: 1090-2104

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Abstract

The hepatic monooxygenase systems largely responsible for the biotransformation of drugs and other xenobiotics are comprised of NADPH-cytochrome P-450 reductase and multiple forms of cytochrome P-450. Optimal temperatures for these systems in the trout and rat are 26° and 37°, respectively. Purified trout and rat reductases are optimally functional at 26° and 37°, respectively, when added to trout and rat microsomes. However, rat reductase was shown to function optimally at 26° when added to trout microsomes and trout reductase functioned optimally at 37° when added to rat microsomes. Corresponding shifts in optimal temperatures of cytochrome P-450-linked 0-deethylation of 7-ethoxycoumarin occurred when these reductases were added to rat or trout microsomes. It is proposed that the phospholipid annulus surrounding the active site of membrane-bound cytochrome P-450 determines the optimal temperature of cytochrome P-450 systems.

Item Type:	Article
Subjects:	Tuberculosis > Laboratory Research > Biochemical
Divisions:	Basic Science Research > Biochemistry
Depositing User:	Dr. Rathinasabapati R
Date Deposited:	12 Aug 2013 07:01
Last Modified:	17 Mar 2016 09:00
URI:	http://eprints.nirt.res.in/id/eprint/190

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