Purification of Membrane-Bound Catechol-O-Methyltransferase
Catechol-0-methyltransferase (COMT, EC 184.108.40.206) was first detected in rat liver extracts (1) and since then, COMT has been found in plants, yeast, invertebrates, and vertebrates. In mammals, the highest COMT activities are encountered in liver, kidney, and gut wall (2,3). The general physiological function of COMT is the inactivation of biologically active or toxic catechols. The enzyme catalyzes the transference of a methyl group from S-adenosyl-l-methionine (SAM) to a hydroxyl group on a catechol substrate in the presence of magnesium and the reaction products are the O-methylated catechol and S-adenosyl-l-homocysteine (1).
KeywordsEthylene Diamine Tetraacetic Acid Ethylene Diamine Tetraacetic Acid Fast Protein Liquid Chromatography COMT Activity Octyl Sulfate
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