Acid phosphatase activity demonstrated by intact Angiostrongylus cantonesis with special reference to its function.

Abstract

Intact Angiostrongylus cantonensis is able to hydrolyse glucose-phosphate esters, mononucleotides and rho-nitrophenyl phosphate as well as beta-glycerophosphate in vitro. Reciprocal inhibition studies suggest that the hydrolysis of such substrates is due to a non-specific phosphomonoesterase. Molybdate ions, which exert no effect on either the uptake of glucose or the production of lactate, inhibit the hydrolysis of glucose-1-phosphate in the external medium and simultaneously lower the production of lactate by the intact worms in vitro.