Hurst J H, Guchhait R B, Billingsley M L, Stolk J M, Lovenberg W
Biochem Biophys Res Commun. 1983 May 16;112(3):1061-8. doi: 10.1016/0006-291x(83)91726-6.
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.
苯乙醇胺N-甲基转移酶的标准纯化程序通过添加利用固定化S-腺苷-L-高半胱氨酸的亲和色谱步骤和使用制备性等电聚焦进行了改进。源自牛肾上腺髓质的酶与S-腺苷-L-高半胱氨酸琼脂糖结合，可用0.1M NaCl洗脱。高达10mM的S-腺苷-L-甲硫氨酸浓度在洗脱该酶时无效。牛苯乙醇胺N-甲基转移酶的制备性等电聚焦显示出一个单一峰，其pI = 4.95。讨论了固定化S-腺苷-L-高半胱氨酸在从其他甲基转移酶中差异分离苯乙醇胺N-甲基转移酶方面的潜在用途。
