Eukaryotic aminoacyl-tRNA synthetases tend to occur in high molecular weight multienzyme complexes in contrast to the prokaryotic counterparts. The functional significance of complex formation is not understood but stabilization of enzyme activities in the complex(es) has been suggested as one of many possible functions. We provide evidence that the 24S complex lysyl-tRNA synthetase activity is more resistant to thermal inactivation than the 6S free lysyl-tRNA synthetase activity at 30°, 37°, and 43°C.
|Original language||English (US)|
|Number of pages||4|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - May 14 1982|
ASJC Scopus subject areas
- Molecular Biology