Biopolym. Cell. 1992; 8(3):6-9.
http://dx.doi.org/10.7124/bc.00031D
Structure and Function of Biopolymers
Effect of ribosomes on the thermostability of rabbit liver aminoacyl-tRNA synthetases
1Sana Sara, 1Ivanov L. L., 1Turkovskaya G. V., 2Martinkus Z. P., 1Kovalenko M. I., 1El'skaya A. V.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680
  2. Kaunas Medical Academy
    Mizkevicha Str. 9, Kaunas, Lithuania, 44307

Abstract

The thermostability of free and associated with polyribosomes aminoacyl-tRNA synthetases from rabbit liver has been studied. The enzymes associated with polyribosomes are more stable to heat inactivation than the free ones. The 80S ribosomes as well as the 40S and 60S ribosomal subunits induce an increase in the thermostability of leucyl-tRNA synthetase in the high-molecular-weight comlpex from rabbit liver.
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