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Purification and Properties of Bovine Phenylethanolamine N-Methyltransferase

Richard J. Connett 1 and Norman Kirshner 1

From the 1 From the Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27706

Phenylethanolamine N-methyltransferase (EC 2.1.1) was isolated and purified approximately 60-fold from bovine adrenal medullae. The final product appears homogeneous by column chromatography, electrophoresis, and ultracentrifugation. The enzyme gave a s20,w of 3.0 S with a molecular weight by Sephadex chromatography of 38,000. No cofactors were needed for the reaction. The pH optimum was 7.9 in either Tris or borate buffers. Titration with p-hydroxymercuribenzoate showed that 8.5 moles of sulfhydryl were titrated per mole of enzyme of 38,000 molecular weight and that activity was lost on titration of 2 moles of sulfhydryl groups per mole of enzyme. Kinetic measurements indicated a complex reaction mechanism which is best described as a random binding of substrates with S-adenosylmethionine being kinetically preferred as the first substrate bound.

Submitted on September 15, 1969


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