Copeland E S, Campbell I C, Murphy D L
Biochim Biophys Acta. 1983 Feb 28;743(1):186-94. doi: 10.1016/0167-4838(83)90433-8.
Interactions between a monoamine oxidase (monoamine: oxygen oxidoreductase deaminating, EC 1.4.3.4) obtained from rat liver cytosol by high speed centrifugation and a biologically active, spin labeled analog of amphetamine have been analyzed. The acetylenic monoamine oxidase inhibitors, pargyline and clorgyline, have been used to modulate the binding of spin labeled amphetamine. Broadening of electron spin resonance lines induced by immobilization of the probe on binding has been used to determine the concentration of bound probe. Pargyline was found to inhibit binding of spin labeled amphetamine by cytosolic monoamine oxidase. Bound spin labeled amphetamine was also displaceable by pargyline. In contrast, clorgyline enhanced the binding of spin labeled amphetamine to the cytosolic monoamine oxidase preparation. Inhibition or enhancement of amphetamine binding was very rapid and occurred during the reversible stage of interaction between the enzyme and the acetylenic compounds.
对通过高速离心从大鼠肝脏胞液中获得的单胺氧化酶（单胺：氧氧化还原酶脱氨基，EC 1.4.3.4）与具有生物活性的、自旋标记的苯丙胺类似物之间的相互作用进行了分析。使用乙炔类单胺氧化酶抑制剂优降宁和氯吉兰来调节自旋标记苯丙胺的结合。通过将探针固定在结合物上诱导的电子自旋共振线展宽来确定结合探针的浓度。发现优降宁可抑制胞液单胺氧化酶对自旋标记苯丙胺的结合。结合的自旋标记苯丙胺也可被优降宁取代。相比之下，氯吉兰增强了自旋标记苯丙胺与胞液单胺氧化酶制剂的结合。苯丙胺结合的抑制或增强非常迅速，且发生在酶与乙炔类化合物相互作用的可逆阶段。
