PMID: 4150Jan 1, 1975

Complete purification and studies on the structural and kinetic properties of two forms of yeast valyl-tRNA synthetase

D KernJ P Ebel


Two forms of baker's yease valyl-tRNA synthetase have been purified to apparent homogeneity by classical methods. It was demonstrated that one of the two forms of the enzyme originates from the other by proteolysis, the respective amounts of each form depending on the physiological state of the yeast. The species mainly isolated from exponential growing yeast cells is a monomer of 130,000 daltons molecular weight. In stationary phase cells or in commercial yeast the major species is a degraded monomer of 120,000 daltons molecular weight ; however when the purification is carried out in the presence of phenylmethyl-sulphonyl fluoride, or diisopropylfluorophosphate large amounts of the not - degreded monomer can be obtained. Of great practical usefulness is the fact that large amounts of the native enzyme can be obtained pure after only two chromatographic steps on DEAE-cellulose and hydroxylapatite. The kinetic constants for valine, ATP and tRNAVal were determined, as well as the optimum aminoacylation conditions. It was found that the specific activity of the nondegraded valyl-tRNA synthetase is higher than that of the proteolysed enzyme for the aminoacylation reaction. On the contrary, both forms have the same ATP-pyroposphate...Continue Reading


Dec 21, 1978·Biochimica Et Biophysica Acta·A DietrichR Giegé
Dec 28, 1981·Biochimica Et Biophysica Acta·E E CreppyG Dirheimer
Nov 1, 1987·Proceedings of the National Academy of Sciences of the United States of America·E RapaportP C Zamecnik
May 1, 1992·Proceedings of the National Academy of Sciences of the United States of America·M FrugierR Giegé
Jul 1, 1977·Nucleic Acids Research·R GiegéG Zaccai
Aug 10, 1979·Nucleic Acids Research·C S LinJ G Chirikjian
Dec 21, 1993·Biochemistry·M FrugierR Giegé
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Nov 1, 1976·European Journal of Biochemistry·A DietrichJ P Ebel
Jun 1, 1987·European Journal of Biochemistry·B LorberR Giegé
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Amino Acyl-tRNA Synthetases
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