Phenylethanolamine N-methyltransferase: Notes on its purification from bovine adrenal medulla and separation from protein carboxymethyltransferase

Jeffrey H. Hurst, Ras B. Guchhait, Melvin L. Billingsley, Jon M. Stolk, Walter Lovenberg

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6 Scopus citations

Abstract

Standard procedures for the purification of phenylethanolamine N-methyltransferase were modified by the addition of an affinity chromatography step utilizing immobilized S-adenosyl-L-homocysteine and by use of preparative isoelectric focusing. Enzyme derived from bovine adrenal medullae was bound to S-adenosyl-L-homocysteine agarose, and could be eluted with 0.1 M NaCl. Concentrations of S-adenosyl-L-methionine as high as 10 mM were ineffective in eluting the enzyme. Preparative isoelectric focusing of bovine phenylethanolamine N-methyltransferase showed a single peak with the pI = 4.95. The potential use of immobilized S-adenosyl-L-homocysteine in the differential separation of phenylethanolamine N-methyltransferase from other methyltransferase enzymes is discussed.

Original languageEnglish (US)
Pages (from-to)1061-1068
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume112
Issue number3
DOIs
StatePublished - May 16 1983

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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