Obata T, Egashira T, Yamanaka Y
Department of Pharmacology, Medical College of Oita, Japan.
Biochem Pharmacol. 1990 Oct 15;40(8):1689-93. doi: 10.1016/0006-2952(90)90343-j.
Monkey platelet monoamine oxidase (MAO) was preferentially found as the B-form of the enzyme as observed from differences in substrate specificities, as well as liver MAO. The isoelectric points and molecular weights of platelet MAO subunits were compared with those of monkey liver using sodium dodecyl sulfate-disc polyacrylamide gel electrophoresis and isoelectric focusing-disc gel electrophoresis. The pI value of monkey liver was a single peak at 6.5, but the pI values of monkey platelets were triple peaks at 5.5, 6.5 and 7.0. The molecular weight of MAO subunits in monkey platelets was similar to that of liver, and was found to be about 60,000. These results indicate that MAO-B of monkey platelets differs from MAO-B of the liver, and that it has different electrophoretic properties.
从底物特异性差异以及肝脏单胺氧化酶（MAO）来看，优先发现猴血小板MAO为该酶的B型。使用十二烷基硫酸钠-圆盘聚丙烯酰胺凝胶电泳和等电聚焦-圆盘凝胶电泳，将血小板MAO亚基的等电点和分子量与猴肝脏的进行比较。猴肝脏的pI值在6.5处为单峰，但猴血小板的pI值在5.5、6.5和7.0处为三峰。猴血小板中MAO亚基的分子量与肝脏的相似，约为60,000。这些结果表明，猴血小板的MAO-B与肝脏的MAO-B不同，且具有不同的电泳特性。
