Reformation of leucyl-tRNA synthetase complexes in revertants from CHO mutant tsH1.
A direct correlation was found to exist between increased thermolability of leucyl-tRNA synthetase and loss of the high-molecular-weight enzyme complexes in the CHO cell mutant tsH1 and its revertants. This was shown to occur apart from a differential thermostability between the complexes themselves and is supported by Michaelis constant determinations.
D000604:Amino Acyl-tRNA Synthetases / Q000235:genetics*; D000818:Animals; D002460:Cell Line; D006224:Cricetinae; D003412:Cricetulus; D004355:Drug Stability; D005260:Female; D014644:Genetic Variation; D007700:Kinetics; D007935:Leucine-tRNA Ligase / Q000235:genetics* / Q000378:metabolism; D046911:Macromolecular Substances; D008970:Molecular Weight; D009154:Mutation; D010053:Ovary; D013696:Temperature
D046911:Macromolecular Substances; D000604:Amino Acyl-tRNA Synthetases; D007935:Leucine-tRNA Ligase