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Molecular Pharmacology, Vol 6, 78-84, Copyright © 1970 by the American Society for Pharmacology and Experimental Therapeutics

Heterogeneity of N- and O-Methyltransferases

JULIUS AXELROD 1 and ELLIOT S. VESELL 1

1 Laboratory of Clinical Science, National Institute of Mental Health, and Laboratory of Chemical Pharmacology, National Heart Institute, National Institutes of Health, Bethesda, Maryland 20014

The methyltransferases phenylethanolamine N-methyltransferase, histamine N-methyltransferase (EC 2.1.1.8), catechol O-methyltransferase (EC 2.1.1.6), and hydroxyindole O-methyltransferase, from tissues of several species, were subjected to starch block electrophoresis. Adrenal phenylethanolamine N-methyltransferase and pineal hydroxyindole O-methyltransferase were heterogeneous among different species with respect to electrophoretic mobility on starch block, heat stability, and substrate specificity, but they were homogeneous within a given species. Multiple forms of histamine N-methyltransferase and catechol O-methyltransferase occurred in tissues within a given species as well as among different species. They had different electrophoretic mobilities, heat stabilities, and kinetic properties.

Note:
ACKNOWLEDGMENTS We thank Dorothy M. Rutherford and Wallace W. Holland for their excellent technical assistance.

Submitted on July 2, 1969




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J. Axelrod
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