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Journal of Pharmacology And Experimental Therapeutics, Vol. 143, Issue 1, 1-6, 1964
Copyright © 1964 by American Society for Pharmacology and Experimental Therapeutics

S-DEMETHYLATION BY MICROSOMAL ENZYMES

Paul Mazel 1, J. Frank Henderson 1, and Julius Axelrod 2

1 Department of Pharmacology, The George Washington University School of Medicine, Washington, D. C.
2 Laboratory of Clinical Science, National Institute of Mental Health, Bethesda, Maryland

The removal of methyl groups from thioethers to yield formaldehyde and free thiols by rat liver microsomal enzymes has been demonstrated. S-Demethylation requires NADP, glucose-6-phosphate, Mg++, nicotinamide, oxygen, microsomes and a soluble NADPH-generating system. NAD does not substitute for NADP. This reaction occurs predominantly in liver, but also to a very small extent in kidney and spleen. A variety of compounds of the type R—S—CH3 are S-demethylated, including compounds in which R is a purine, hydrogen, a barbiturate, benzothiazole, an amino acid and an amidine. Rat, rabbit, and mouse liver preparations demethylated 6-methylthiopurine and methylthiopseudourea, but to different degrees suggesting more than one S-demethylating enzyme. There was no significant difference in S-demethylation between male and female rats.

Submitted on July 1, 1963
Accepted on September 18, 1963




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Copyright © 1964 by the American Society for Pharmacology and Experimental Therapeutics.