猪心脏线粒体天冬氨酸氨基转移酶的去折叠及复性尝试
The unfolding and attempted refolding of mitochondrial aspartate aminotransferase from pig heart.
作者信息
West S M, Price N C
机构信息
School of Molecular and Biological Sciences, University of Stirling, Scotland, U.K.
出版信息
Biochem J. 1990 Jan 1;265(1):45-50. doi: 10.1042/bj2650045.
Abstract
The unfolding of the mitochondrial isoenzyme of aspartate aminotransferase from pig heart in solutions of guanidinium chloride (GdnHCl) has been studied. By a number of criteria (enzyme activity, protein fluorescence, c.d., thiol-group reactivity), the enzyme was judged to be almost completely unfolded in 2 M-GdnHCl. On dilution of the GdnHCl, no re-activation of the enzyme could be observed, whether or not pyridoxal 5'-phosphate and dithiothreitol were present. The behaviour of the mitochondrial isoenzyme is in marked contrast with that of the cytoplasmic isoenzyme [West & Price (1989) Biochem. J. 261, 189-196], despite the similarities in the amino acid sequences and tertiary structures of the two isoenzymes. The implications of these findings for the process of folding and assembly of the mitochondrial isoenzyme in vivo are discussed.
摘要
对猪心中天冬氨酸氨基转移酶的线粒体同工酶在氯化胍（GdnHCl）溶液中的去折叠过程进行了研究。根据多种标准（酶活性、蛋白质荧光、圆二色性、巯基反应性）判断，该酶在2M - GdnHCl中几乎完全去折叠。稀释GdnHCl时，无论是否存在磷酸吡哆醛5'-磷酸和二硫苏糖醇，均未观察到酶的重新激活。尽管两种同工酶的氨基酸序列和三级结构相似，但线粒体同工酶的行为与细胞质同工酶的行为形成了显著对比。讨论了这些发现对线粒体同工酶在体内折叠和组装过程的影响。
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