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PARTIAL PURIFICATION OF DROSOPHILA GLUTAMATE DECARBOXYLASE 1

Abstract— A 600‐fold purification of l‐glutamatc decarboxylasc from Drosophila melanogaster Oregon R Wild Type has been achieved. The purification procedures involve the initial homogenization of whole flies in dilute potassium phosphate buffer containing dithiothreitol and phenylmethyl sulfonyl fluoride as protectors, followed by a series of column chromatography with hydroxylapatite, Sephadex G‐150 and DEAE‐Sephadex. The purified enzyme has an apparent Km of 11 mm for l‐glutamate and requires a 40mm‐K+ for maximum activity.