胺氧化酶对光学活性底物和抑制剂的特异性。
Specificity of amine oxidase for optically active substrates and inhibitors.
作者信息
PRATESI P, BLASCHKO H
出版信息
Br J Pharmacol Chemother. 1959 Jun;14(2):256-60. doi: 10.1111/j.1476-5381.1959.tb01395.x.
A number of optically active amines have been tested as substrates or inhibitors of amine oxidase of rabbit and guinea-pig liver. The two stereoisomers of beta-hydroxyphenethylamine were oxidized at the same rate by rabbit liver, but the guinea-pig liver extracts oxidized the D form more rapidly than the L form. The two stereoisomers of amphetamine were equally active as inhibitors of the rabbit liver oxidase, but with guinea-pig liver extracts dexamphetamine, the (+) form, was more potent as an inhibitor. In both species, 2-hydroxy-1-phenylethylamine was a weaker inhibitor than 1-phenylethylamine; in the rabbit liver (+) forms of these two amines were more potent as inhibitors.
已对多种旋光性胺作为兔和豚鼠肝脏胺氧化酶的底物或抑制剂进行了测试。β-羟基苯乙胺的两种立体异构体被兔肝脏以相同速率氧化，但豚鼠肝脏提取物氧化D型的速度比L型更快。苯丙胺的两种立体异构体作为兔肝脏氧化酶的抑制剂活性相同，但对于豚鼠肝脏提取物，右旋苯丙胺，即(+)型，作为抑制剂更有效。在这两个物种中，2-羟基-1-苯乙胺作为抑制剂比1-苯乙胺弱；在兔肝脏中，这两种胺的(+)型作为抑制剂更有效。
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