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Purification and properties of two membrane alkaline phosphatases from Bacillus subtilis 168
1Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University, Sendai, Japan.
Journal of Bacteriology
|March 1, 1991
Abstract:
Two alkaline phosphatases were extracted from the membranes of Bacillus subtilis 168 stationary-phase cells and purified as homogeneous proteins by hydroxyapatite column chromatography. Alkaline phosphatases I and II differed in several properties such as subunit molecular weight, substrate specificity, thermostability, Km, pH stability, and peptide maps.