Multiple forms of alkaline phosphatase from Escherichia coli cells with repressed and derepressed biosynthesis of the enzyme

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Abstract
Isolation of multiple forms of alkaline phosphatase [EC 3.1.3.1] from E. coli cells with repressed and derepressed biosyntheses of the enzyme is reported. Three enzyme forms were isolated from cells with derepressed synthesis and 1 form was isolated from cells with repressed enzyme synthesis. The multiple enzyme forms did not differ in pH optimum, thermostability or the degree of inhibition with orthophosphate; they did differ in the relative rate of hydrolysis of different substrates. The addition of substrates to the cells during enzyme derepression resulted in changes of the ratio of the multiple forms.