Molecular characteristics of human platelet monoamine oxidase.

The monoamine oxidase B (MAO-B) selective inhibitor J-508 (N-methyl-N-propargyl-(1-indanyl)-ammonium chloride) appears to interact with MAO-B in a manner consistent with a "suicide" reaction. Because of this property, J-508 could be used, under the appropriate conditions, to "titrate" the concentration of MAO-B active centres in the human platelet, although some non-specific binding of this compound to sites other than the active centre of this enzyme form was found, thus limiting the accuracy of the titration method. The molecular characteristics of human platelet MAO-B (Km, Vmax, approximate enzyme concentrations and molecular turnover members) towards three of its monoamine substrates have been estimated. The natural variation of platelet MAO-B activity from individual to individual is due to a variation in the Vmax without a variation in the Km towards benzylamine is substrate, and is based, at least in part, upon a variation in the concentration of this enzyme form.