兔肝精氨酰 - tRNA合成酶高分子量和低分子量形式的热稳定性及疏水特性比较

Comparison of the thermolability and hydrophobic properties of high- and low-molecular-weight forms of rabbit liver arginyl-tRNA synthetase.

作者信息

Berbeć H, Paszkowska A

机构信息

Department of Physiological Chemistry, Medical School, Lublin, Poland.

出版信息

Mol Cell Biochem. 1989 Apr 11;86(2):125-33. doi: 10.1007/BF00222612.

DOI:10.1007/BF00222612

PMID:2770710

Abstract

Two preparations with arginyl-tRNA synthetase activity have been obtained from rabbit liver post-microsomal fraction: a) a high-molecular-weight containing the multienzyme aminoacyl-tRNA synthetase complex and b) a low-molecular-weight preparation containing free enzymes. Thermal inactivation of arginyl-tRNA synthetase in both preparations has been compared in a solution which was successively supplemented with tRNA, reduced glutathione, L-ascorbic acid, ZnCl2 and Triton X 100. Moreover, hydrophobic properties of both enzyme preparations have been compared. It was found that the complexed arginyl-tRNA synthetase is more stable than the free enzyme. A role of hydrophobic interactions in the maintenance of the complexed enzyme stability is suggested.

摘要

已从兔肝微粒体后组分中获得了两种具有精氨酰 - tRNA合成酶活性的制剂：a）一种高分子量制剂，含有多酶氨酰 - tRNA合成酶复合物；b）一种低分子量制剂，含有游离酶。在依次添加了tRNA、还原型谷胱甘肽、L - 抗坏血酸、ZnCl2和Triton X 100的溶液中，对两种制剂中的精氨酰 - tRNA合成酶的热失活进行了比较。此外，还比较了两种酶制剂的疏水特性。结果发现，复合精氨酰 - tRNA合成酶比游离酶更稳定。提示疏水相互作用在维持复合酶稳定性中起作用。