Properties of Alkaline Phosphatase from Bacillus Subtilis

Abstract

An increase in the activity of alkaline phosphatase was observed in an in vitro system containing soluble and particulate fractions from Bacillus Subtills (Whiteley and Oishi, 1963). In order to determine whether the increase was due to activation of preformed enzyme or enzyme synthesis , a study of the properties of the enzyme was required. Although alkaline phosphatase was found to be an exoenzyme in B. subtilis (Cashel and Freese, 1964) , little was known about the other properties of the enzyme. In contrast, the alkaline phosphatase of Escherichia coli has been studied extensively. The properties of a highly purified enzyme, mechanism of action, localization of the enzyme in the cell, as well as the genetics and regulation of enzyme synthesis have been investigated. In addition, in vitro synthesis of alkaline phosphatase has also been reported (Bishop, et al,1964; Manson, et all, 1965). Because of the possible influence of these findings on the problem of enzyme activation or synthesis in B. subtils, information concerning the E. coli enzyme will be reviewed briefly.