Literature DB >> 6661237

Hydrodynamic properties and structure of the rat liver 12 S arginyl- and lysyl-tRNA synthetase complex.

C V Dang, C V Dang.   

Abstract

Eukaryotic aminoacyl-tRNA synthetases occur in multienzyme complexes in contrast to their prokaryotic counterparts. A core 12 S rat liver complex (Mr 290,000) was recently purified to homogeneity consisting of two polypeptides with Mr 73,000 and 65,000 identified as lysyl- and arginyl-tRNA synthetase, respectively (Dang et al. (1982) Biochemistry 21,1959-1966). Using the modified hydrodynamic theory of Kirkwood (Kirkwood, J.R. (1954) J. Polym. Sci. 12,1-14), we have determined that the model most consistent with the hydrodynamic properties of the 12 S complex is a tetrameric tetrahedral model.

Entities:  

Mesh:

Substances:

Year:  1983        PMID: 6661237     DOI: 10.1016/0006-291x(83)91223-8

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  3 in total

Review 1.  Higher eukaryotic aminoacyl-tRNA synthetases in physiologic and pathologic states.

Authors:  C V Dang; C V Dang
Journal:  Mol Cell Biochem       Date:  1986-08       Impact factor: 3.396

Review 2.  Multienzyme complex of aminoacyl-tRNA synthetases: an essence of being eukaryotic.

Authors:  C V Dang; C V Dang
Journal:  Biochem J       Date:  1986-10-15       Impact factor: 3.857

3.  Structural organization of high-Mr mammalian aminoacyl-tRNA synthetases. Comparison of multi-enzyme complexes from different sources.

Authors:  C V Dang; C V Dang
Journal:  Mol Cell Biochem       Date:  1984-09       Impact factor: 3.396

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.