ABSTRACT
Enzymes of catecholamine biosynthesis, tyrosine hydroxylase (TH), aromatic L-amino acid decarboxylase (AADC), dopamine ß-hydroxylase (DBH), and phenyl-ethanolamine N-methyltransferase (PNMT), have been extensively studied in biochemistry, pharmacology, physiology, and neurobiology. High-performance liquid chromatography (HPLC) has been extensively developed, and great advances have also been made in the study of enzymes and proteins by HPLC. Among catecholamine-related enzymes, only TH and monoamine oxidase type B have been tried to purify using a HPLC step. TH of rabbit adrenals was subjected on gel filtration-HPLC and monoamine oxidase of human platelet on anion exchange HPLC. The application of HPLC for enzyme purification is developing rapidly. Although the experiments shown are only a few examples, the results prove that HPLC is quite useful for analysis and purification of catecholamine-related enzymes. In this HPLC system, four catecholamine-synthesizing enzymes (TH, AADC, DBH, and PNMT) were almost completely separated with apparent Mr which agree with the reported values.
