Purification and partial characterization of mammalian Cu-dependent amine oxidases.

G Houen, J Jørgensen, L Leonardsen, L I Larsson
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引用次数: 10

Abstract

Bovine serum amine oxidase, porcine kidney diamine oxidase and human placental and pregnancy serum diamine oxidases have been purified by affinity chromatography and ion exchange chromatography. The purified enzymes were subjected to peptide mapping studies with trypsin, S. aureus V8 protease and pepsin. These studies revealed similarities between the enzymes and partial sequences from the bovine serum amine oxidase were obtained. The sequences obtained showed no homology to known sequences. Immunological studies using monoclonal antibodies to the purified enzymes revealed cross reactivity between the four enzymes. These results support the view that the Cu-dependent amine oxidases constitute a closely related group (E.C. 1.4.3.6).

哺乳动物铜依赖胺氧化酶的纯化和部分特性。
牛血清胺氧化酶、猪肾二胺氧化酶和人胎盘和妊娠血清二胺氧化酶分别用亲和层析和离子交换层析纯化。纯化的酶与胰蛋白酶、金黄色葡萄球菌V8蛋白酶和胃蛋白酶进行肽定位研究。这些研究揭示了酶与牛血清胺氧化酶的部分序列之间的相似性。所得序列与已知序列无同源性。使用纯化酶的单克隆抗体进行免疫学研究,发现这四种酶之间存在交叉反应性。这些结果支持了铜依赖胺氧化酶构成一个密切相关的基团的观点(E.C. 1.4.3.6)。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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