Comparison of the thermolability and hydrophobic properties of high- and low-molecular-weight forms of rabbit liver arginyl-tRNA synthetase |
| |
Authors: | Henryk Berbeć Alicja Paszkowska |
| |
Institution: | (1) Department of Physiological Chemistry, Medical School, Lubartowska 85, 20-123 Lublin, Poland |
| |
Abstract: | 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.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 |
| |
Keywords: | arginyl-tRNA synthetase multienzyme complex rabbit liver |
本文献已被 SpringerLink 等数据库收录! |
|