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

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Summary

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 × 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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Abbreviations

DFP:

Diisopropylfluorophosphate

GSH:

Glutathione (reduced)

PMSF:

Phenylmethylsulfonyl Fluoride

Ap4A:

Diadenosine 5′, 5″-P1, P4-tetraphosphate

Preparation I:

high-molecular-weight arginyl-tRNA synthetase preparation

Preparation II:

low-molecular-weight arginyl-tRNA synthetase preparation

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  1. Department of Physiological Chemistry, Medical School, Lubartowska 85, 20-123, Lublin, Poland

    Henryk Berbeć & Alicja Paszkowska

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  1. Henryk Berbeć
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  2. Alicja Paszkowska
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Berbeć, H., Paszkowska, A. Comparison of the thermolability and hydrophobic properties of high- and low-molecular-weight forms of rabbit liver arginyl-tRNA synthetase. Mol Cell Biochem 86, 125–133 (1989). https://doi.org/10.1007/BF00222612

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  • DOI: https://doi.org/10.1007/BF00222612

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