来自单峰驼蜱（Hyalomma dromedarii）发育胚胎中天冬氨酸转氨酶的纯化与特性分析
Purification and characterization of aspartate aminotransferase from developing embryos of the camel tick Hyalomma dromedarii.
作者信息
Mohamed T M
机构信息
Molecular Biology Department, National Research Centre, Dokki, Cairo, Egypt.
出版信息
Exp Appl Acarol. 2001;25(3):231-44. doi: 10.1023/a:1010618203054.
Aspartate transaminase (AST) activity in the camel tick Hyalomma dromedarii was followed throughout embryogenesis. During purification of AST to homogeneity, ion exchange chromatography lead to four separate forms (termed I, II, III and IV). AST II with the highest specific activity was pure after chromatography on Sephacryl S-300. The molecular mass of AST II was 52 KDa for the native enzyme, composed of one subunit of 50 KDa. AST II had a Km value of 0.67mM for a-ketoglutarate and 15.1 mM for aspartate. AST II had a pH optimum of 7.5 with heat stability up to 50 degrees C for 15 min. The enzyme was activated by MnCl2, and inhibited by CaCl2, MgCl2. NiCl2, and ZnCl2.
在整个胚胎发育过程中，对骆驼蜱（Hyalomma dromedarii）中的天冬氨酸转氨酶（AST）活性进行了跟踪研究。在将AST纯化至同质的过程中，离子交换色谱法产生了四种不同的形式（分别称为I、II、III和IV）。在Sephacryl S - 300上进行色谱分离后，具有最高比活性的AST II达到了纯品状态。天然酶AST II的分子量为52 kDa，由一个50 kDa的亚基组成。AST II对α - 酮戊二酸的Km值为0.67 mM，对天冬氨酸的Km值为15.1 mM。AST II的最适pH值为7.5，在50摄氏度下具有15分钟的热稳定性。该酶被MnCl2激活，并被CaCl2、MgCl2、NiCl2和ZnCl2抑制。
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