TY - JOUR
T1 - Hydrodynamic properties and structure of the rat liver 12 S arginyl- and lysyl-tRNA synthetase complex
AU - Dang, Chuan V.
AU - Dang, Chi V.
PY - 1983/12/16
Y1 - 1983/12/16
N2 - 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.
AB - 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.
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U2 - 10.1016/0006-291X(83)91223-8
DO - 10.1016/0006-291X(83)91223-8
M3 - Article
C2 - 6661237
AN - SCOPUS:0021106512
SN - 0006-291X
VL - 117
SP - 464
EP - 469
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -