Multiple Forms of Lysyl-tRNA Synthetase fromEscherichia coli
- 1 January 1976
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 357 (1), 543-552
- https://doi.org/10.1515/bchm2.1976.357.1.543
Abstract
Lysyl-tRNA synthetase was isolated from E. coli. The enzymatic activity elutes as 3 or 4 bands from a hydroxylapatite column. Polyacrylamide gel analysis shows that each of these bands contains more than 1 enzymatically active protein species. The MW of the subunits of these species provide an explanation for the variation in the MW previously reported for this enzyme.This publication has 4 references indexed in Scilit:
- A study of lysyl-ribonucleic acid synthetase in relation to substrate conformationArchives of Biochemistry and Biophysics, 1967
- Purification and properties of lysyl-sRNA synthetase from Escherichia coliCollection of Czechoslovak Chemical Communications, 1965
- Sulfonyl Fluorides as Inhibitors of Esterases. I. Rates of Reaction with Acetylcholinesterase, α-Chymotrypsin, and TrypsinJournal of the American Chemical Society, 1963