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

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

H Berbeć  1 , A Paszkowska
Affiliations

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

H Berbeć et al. Mol Cell Biochem. .

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.

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