Abstract
A procedure is described for obtaining an improved purification of catechol- O-methyltransferase. The molecular weight of the enzyme is estimated to be 29,000 from its behavior on Sephadex G-100. The presence of multiple bands of activity after polyacrylamide gel electrophoresis is reported. It is shown that all catechols are substrates of the enzyme, but that 4-nitrocatechol can act as a non-competitive inhibitor of the O-methylation of another catechol.
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