重组人聚adp核糖聚合酶(PARP)在酵母中的表达及纯化。与大鼠酶的药理特征比较。

D Perrin, S Gras, B van Hille, B T Hill
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引用次数: 7

摘要

在GAL启动子的控制下,人多adp核糖聚合酶(PARP)在酵母细胞系JEL1中表达。提取蛋白,纯化人重组PARP,均质性明显。这种人类酶的药理学特征是根据属于不同化学家族的已知PARP抑制剂的作用来表征的,并将其与使用相同纯化方案从大鼠睾丸中纯化的大鼠酶进行比较。大鼠和人类的酶对这些选定的抑制剂的敏感性似乎非常相似。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Expression in yeast and purification of functional recombinant human poly(ADP-ribose)polymerase (PARP). Comparative pharmacological profile with that of the rat enzyme.

Human poly(ADP-ribose)polymerase (PARP) was expressed in the yeast line JEL1 under the control of a GAL promoter. Proteins were extracted and human recombinant PARP purified to apparent homogeneity. The pharmacological profile of this human enzyme was characterised in terms of the effects of known inhibitors of PARP belonging to various chemical families and this was compared with that of the rat enzyme purified from rat testes, using the same purification protocol. The rat and the human enzymes appeared very similar in terms of their sensitivities to those selected inhibitors.

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