Silverman R B
J Biol Chem. 1983 Dec 25;258(24):14766-9.
Mitochondrial monoamine oxidase was inactivated with 2-[2-14C]phenylcyclopropylamine, dialyzed, and treated with acidic 2,4-dinitrophenylhydrazine. Contrary to the report of Paech et al. (Paech, C., Salach, J. I., and Singer, T. P. (1980) J. Biol. Chem. 255, 2700-2704), the 2,4-dinitrophenylhydrazone obtained was not that of 2-phenylcyclopropanone, but rather of cinnamaldehyde. Furthermore, denaturation of the labeled enzyme in the presence of sodium borohydride resulted in retention of 5.6 times more radioactivity than in its absence. Based on these results, a mechanism of inactivation of monoamine oxidase by 2-phenylcyclopropylamine and the structure of the enzyme-inactivator adduct are proposed.
用2-[2-¹⁴C]苯基环丙胺使线粒体单胺氧化酶失活，透析后，用酸性2,4-二硝基苯肼处理。与Paech等人的报告（Paech, C., Salach, J. I., and Singer, T. P. (1980) J. Biol. Chem. 255, 2700 - 2704）相反，得到的2,4-二硝基苯腙不是2-苯基环丙酮的，而是肉桂醛的。此外，在硼氢化钠存在下标记酶的变性导致保留的放射性比不存在时多5.6倍。基于这些结果，提出了2-苯基环丙胺使单胺氧化酶失活的机制以及酶-失活剂加合物的结构。
