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Species Differences in Inducibility of Phenylethanolamine-N-Methyl Transferase

Department of Nutrition and Food Science, Massachusetts Institute of Technology Cambridge, Massachusetts
National Institute of Mental Health, National Heart Institute, National Cancer Institute, National Institutes of Health Bethesda, Maryland

Abstract

In the rat, the enzyme that methylates norepinephrine to form epinephrine, phenylethanolamine-N-methyl transferase (PNMT), is highly localized in the adrenal medulla. Its activity is controlled by steroid hormones from the adrenal cortex. Frog PNMT differs from the rat enzyme in its pH, ionic strength, and temperature optima, its thermolability, stability in cold, dilute buffer, and rate of migration on starch-block electrophoresis. The substrate specificities of both enzymes are similar, and both are stimulated in vitro by ethylenediamine tetra-acetate (EDTA), and inhibited by tranylcypromine. Unlike the rat enzyme, frog PNMT activity is present in many organs, and does not decline following hypophysectomy. It is suggested that frog PNMT is an uninducible form of the rat enzyme. (Endocrinology 82: 584, 1968)

Footnotes

Supported in part by USPHS Grant AM-11237.

Received October 11, 1967.

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