紫贻贝(Mytilus galloprovincialis Lam)套膜组织中天冬氨酸转氨酶的部分纯化及其性质。

Özlem Dönmez Yurtpınar
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引用次数: 2

摘要

谷草转氨酶(E.C.2.6.1.1;AST是一种吡哆醛磷酸依赖酶,几乎存在于所有生物体中,在中间氮代谢中起关键作用。虽然AST是从多种植物和动物中纯化出来的,但以前还没有从贻贝(Mytilus galloprovincialis Lam)的套膜组织中纯化过。在本研究中,我们从牛毛霉的套膜组织中部分纯化了AST,并研究了该酶的一些动力学性质。部分纯化的酶在聚丙烯酰胺凝胶电泳中显示出三个蛋白和一个活性带。结果表明,该酶在15oC和35oC时活性最高,在40oC时活性下降,在55oC时活性完全丧失。Tris-HCl缓冲液在pH 7.4时AST活性最高。AST对天冬氨酸和2-氧葡萄糖酸盐的Km值分别为1.64 mM和2.2x10-2 mM,对相同底物的Vmax值分别为0.12 U/mL和0.168 U/mL
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Partial purification and some properties of aspartate aminotransferase from the mantle tissue of Mytilus galloprovincialis Lam.
Aspartate aminotransferase (E.C.2.6.1.1; AST), is a pyridoxal phosphate dependent enzyme that occurs in virtually all organisms and plays a key role in intermediary nitrogen metabolism. Although AST was purified from a variety of plant and animal sources, it has not been purified previously from mantle tissue of Mytilus galloprovincialis Lam. In the present study we have partially purified AST from the mantle tissue of M. galloprovincialis and investigated some kinetic properties of the enzyme. The partially purified enzyme showed three protein and a single activity band in polyacrylamide gel electrophoresis. It was found that the enzyme exhibited maximum activity at 15oC and 35oC and that the activity was decreased at 40oC and totally lost at 55oC. AST activity was maximum at pH 7.4 in Tris-HCl buffer. Km values of AST for aspartate and 2-oxoglutarate were 1.64 mM and 2.2x10-2 mM, respectively, and Vmax values for the same substrates were 0.12 U/mL and 0.168 U/mL, respectively
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