The adaptive d-glycerate 3-kinase from glycerate-adapted Escherichia coli has been purified 4200-fold in 37% yield and has been crystallized. The procedure, starting with the crude, cell-free extract, consisted of treatment with protamine sulfate, ammonium sulfate, passage through a diethylaminoethyl Sephadex column, and precipitation with ethanol. The reaction product, 3-phosphoglycerate, has been identified by paper chromatography and specific enzymatic assay. Some characteristics of the enzyme which show clearly its differences from other glycerate kinases are described.
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Doughty et al. (1966) studied this question.
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