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The extraedlular adenine deaminase from Nocardioides sp. J-275L was purified by the following techniques: ammonium sulfate fractionation, DEAE-Cellulose, DEAE-Sephadex A-50 column chromatography, and Sephacryl S-200 superfine gel filtration. The enzyme was partially purified about 31189-15-fold with about 5.2% yield by these procedur. The molecular weight of the enzyme was 39,000 by a calibrated Sephacryl 5-200 superfine column chromatography. The enzyme was stable at pH 7.5 and up to 40°C. Glycerol was effective on the stabilization of the enzyme during storage. The optimum pH and temperature of the enzyme were around pH 7.5 and 40 °C, respectively. The apparent Michaelis constant Km of the enzyme for adenine was 7.4 x 10-5M. The purine analogues, 6.chloropariae, 2,6-diaminopuriae, 6-bromoparine, 4-aminopyrazolo 13,4-dlpyrimidine, and 0-aaadaiee were substrates for the enzyme. 6-Dimethylaminopurine was a competitive inhibitor of the enzyme. The enzyme was inhibited by 1mM of Cue +, Fe3+, Pb2+, Hg2+, and Ag , and 1mM of a,a´-dipyridyl, pentacblorophenol, and pCMB.
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