Dowling T G, Cambi S, Buffoni F
Department of Pharmacology, University of Florence, Italy.
J Neural Transm Suppl. 1998;52:265-70. doi: 10.1007/978-3-7091-6499-0_26.
A semicarbazide-sensitive amine oxidase (SSAO) (E.C.1.4.3.6) has been purified from pig heart. Western blot analysis showed that the enzyme reacts with a polyclonal antibody raised against homogeneous crystalline pig plasma benzylamine oxidase (BAO). A subunit molecular mass of 97 KDa obtained by SDS electrophoresis is identical to the plasma enzyme. The purification procedure consisted of sequential DEAE cellulose, octyl-Sepharose, Con A-Sepharose and hydroxyapatite columns. Two peaks of activity were obtained on octyl-Sepharose which were found to be kinetically and immunologically indistinguishable. The specific activity of the purified enzyme was 0.045 mumol/min/mg of protein at 37 degrees C and the Km for benzylamine was estimated to be 63 microM. The enzyme was inhibited by carbonyl reagents such as semicarbazide but was insensitive to the effect of pargyline.
已从猪心中纯化出一种氨基脲敏感胺氧化酶（SSAO）（E.C.1.4.3.6）。蛋白质免疫印迹分析表明，该酶与针对纯化的猪血浆苄胺氧化酶（BAO）产生的多克隆抗体发生反应。通过SDS电泳获得的97 kDa亚基分子量与血浆酶相同。纯化过程包括依次使用DEAE纤维素柱、辛基琼脂糖柱、伴刀豆球蛋白A琼脂糖柱和羟基磷灰石柱。在辛基琼脂糖柱上获得了两个活性峰，发现它们在动力学和免疫学上无法区分。纯化酶在37℃时的比活性为0.045 μmol/分钟/毫克蛋白质，苄胺的Km估计为63 μM。该酶被氨基脲等羰基试剂抑制，但对炔丙基胺的作用不敏感。
