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KMID : 0377219840090010083
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Medical Journal of Chosun Univercity
1984 Volume.9 No. 1 p.83 ~ p.94
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Purification and Properties of Alkaline Phospinatase from E. Coli C-90
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Abstract
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An alkaline phosphatase was crystallized from E. coli C-90 and its properties were characterized. The purification procedure involved DEAE-cellulose ion exchange chrornatograpgy. Ninety three-folds purified enzyme was crystallized from ammonium sulfate solution.
The enzyme shoved a maximal activity at pH 9.3. The ㎞ and Vmax for p-nitrophenylphosphate were 4.0 × 10_(-4)M and 2.0 × 10_(-2)IM/min/㎎ protein, respectively. Inorganic phosphate inhibited the enzyme competitively. The molecular weight of the enzyme was 52,000 daltons as determined by acrylamide gel electrophoresis.
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