The purification and properties of adenosine triphosphate-lombricine phosphotransferase

Abstract

A method is described for the preparation, in an electrophoretically homogeneous state, of ATP-lombricine phosphotransferase from the muscular body wall of the earthworm (Megascolides cameroni). The enzyme displayed optimum activity in the forward and reverse reactions at pH 8.6 and 7.2, respectively, and was activated in both directions by Mg2+, Mn2+, Ca2+ or Co2+ ions. The enzyme catalyses the phosphorylation of L-lombricine at a faster rate than that of D-lombricine, the natural substrate. Taurocyamine and 2-guanidinoethyl phosphate can also function as phosphoryl group acceptors. Both ADP and deADP can act as phosphoryl group acceptors. The enzyme is similar in its general characteristics to other previously described ATP-guanidino phos-photransf erases.