Abstract
l-Valyl-sRNA synthetase ( l-valine:sRNA ligase (AMP), EC 6. i. i.9) has been purified from Escherichia coli by a procedure involving autolysis, (NH 4) 2SO 4 fractionation, adsorption on and elution from calcium phosphate gel, and column chromatography. The enzyme, which is about 650-fold purified over the initial cell-free extract, is homogeneous on ultracentrifugation (sedimentation coefficient 4.2 S) and on polyacrylamide-gel electrophoresis. Certain general properties of the enzyme and the effect of various metal ions on its activity have been determined. The enzyme is inhibited by N- ethylmaleimide and p- chloromercuribenzoate . Preliminary studies of the enzyme sulfhydryl groups have been carried out.
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