Phenylethanolamine N-methyltransferase: notes on its purification from bovine adrenal medulla and separation from protein carboxymethyltransferase.
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.
D000313:Adrenal Medulla / Q000201:enzymology*; D000818:Animals; D001921:Brain / Q000201:enzymology; D002417:Cattle; D002846:Chromatography, Affinity; D007525:Isoelectric Focusing; D010625:Phenylethanolamine N-Methyltransferase / Q000302:isolation & purification*; D011496:Protein Methyltransferases / Q000302:isolation & purification*; D011497:Protein O-Methyltransferase / Q000302:isolation & purification*; D051381:Rats
D011496:Protein Methyltransferases; D011497:Protein O-Methyltransferase; D010625:Phenylethanolamine N-Methyltransferase