Purification of the chloroplastic valyl-tRNA synthetase from Euglena gracilis. |
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Authors: | P Imbault V Sarantoglou J H Weil |
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Institution: | Institut de Biologie Moléculaire et Cellulaire, Université Louis Pasteur, 15, rue Descartes, 67084 Strasbourg, France |
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Abstract: | Euglena gracilis chloroplast valyl-tRNA synthetase was purified 990 fold to a specific activity of about 1100 units/mg protein, by a series of steps including ammonium sulfate precipitation and chromatography on hydroxyapatite, DEAE-cellulose, Blue Dextran — Sepharose and Sephadex G200. The enzyme gives a single band upon polyacrylamide gel electrophoresis, appears to be a monomer with a molecular weight of 126,000 daltons and has Km values of 1.5 × 10?5 M for L-valine, 5 × 10?5 M for ATP, and 6 × 10?8 for tRNAVal. |
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