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

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.

journal_name

Mol Cell Biochem

authors

Berbeć H,Paszkowska A

doi

10.1007/BF00222612

subject

Has Abstract

pub_date

1989-04-11 00:00:00

pages

125-33

issue

2

eissn

0300-8177

issn

1573-4919

journal_volume

86

pub_type

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