Yeast mitochondrial and cytoplasmic valyl-tRNA synthetases
Autor: | S. Felter, M. Diatewa, A.J.C. Stahl, C. Schneider |
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Rok vydání: | 1981 |
Předmět: |
Tris
Cytoplasm Valine-tRNA Ligase Biophysics Saccharomyces cerevisiae Mitochondrion Biology Biochemistry Amino Acyl-tRNA Synthetases chemistry.chemical_compound Molecular Biology Ammonium sulfate precipitation chemistry.chemical_classification Chromatography Cell Biology Molecular biology Yeast Mitochondria Molecular Weight Kinetics Enzyme chemistry Transfer RNA Chromatography Gel Electrophoresis Polyacrylamide Gel Hydroxyapatites PMSF |
Zdroj: | Biochemical and Biophysical Research Communications. 98:727-734 |
ISSN: | 0006-291X |
DOI: | 10.1016/0006-291x(81)91173-6 |
Popis: | Yeast mitochondrial tRNA synthetase has been partially purified and chromatographic, catalytic and antigenic properties have been compared to the cytoplasmic homologous enzyme from yeast. No significant differences could be observed between the two enzymes with respect to their behaviour during ammonium sulfate precipitation or in chromatographic separation on DEAE cellulose, hydroxylapatite and Sephadex G 200. The Km of the two enzymes toward tRNAs from yeast mitochondria, yeast cytoplasm or E. coli are pratically identical. The antigenic properties of the two enzymes are very similar; antisera against either the mitochondria or the cytoplasmic enzyme lead to the inhibition of their catalytic properties. The mitochondrial ValRS is formed by a single polypeptide chain whose molecular weight is 125,000 daltons, a value very close to that of the yeast cytoplasmic enzyme. |
Databáze: | OpenAIRE |
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