Reversible heat activation of alkaline phosphatase of Dictyostelium discoideum and its developmental implication

Abstract

The activities of some enzymes increase during the development of the cellular slime mould, Dictyostelium discoideum. Because optimal specific activity is attained by each enzyme at a specific developmental stage¹, development can be followed as a function of enzyme activity. The activity of one of these enzymes, alkaline phosphatase, increases markedly during the late stages of development, making it a potentially useful marker for terminal differentiation^2,3. It has been suggested that this increase in activity is due to de novo enzyme synthesis because the increase in activity does not occur in the presence of inhibitors of RNA and protein synthesis². However, we present evidence here of reversible heat activation of membrane-bound alkaline phosphatase which suggests that the increase in alkaline phosphatase activity may be due to an unmasking of pre-existing enzyme by a novel membrane regulatory mechanism.