Comparison of the thermolability and hydrophobic properties of high- and low-molecular-weight forms of rabbit liver arginyl-tRNA synthetase
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Clinical Biochemistry,Molecular Biology,General Medicine
Link
http://link.springer.com/content/pdf/10.1007/BF00222612.pdf
Reference37 articles.
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2. Dang CV, Dang CV: Multienzyme complexes of eukaryotic aminoacyl-tRNA synthetases. Biosci Rep 3:527–538, 1983
3. Deutscher MP: The eucaryotic amioacyl-tRNA synthetase complex: suggestions for its structure and function. J Cell Biol 99:373–377, 1984
4. Dang CV, Dang CV: Multienzyme complex of aminoacyl-tRNA synthetase: an essence of being eukaryotic. Biochem J 239:249–255, 1986
5. Sihag RK, Deutscher MP: Perturbation of the aminoacyl-tRNA synthetase complex by salts and detergents. Importance of hydrophobic interactions and possible involvement of lipids. J Biol Chem 258:11846–11850, 1983
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1. Mammalian aminoacyl-tRNA synthetases;Current Topics in Cellular Regulation;1996
2. Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents;Journal of Biological Chemistry;1991-08
3. Functional significance of aminoacyl-tRNA synthetase complex in the aminoacylation of tRNALeu isoacceptors;Biochemical and Biophysical Research Communications;1989-08
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