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

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Abstract
Intact Angiostrongylus cantonensis is able to hydrolyse glucose-phosphate esters, mononucleotides and p-nitrophenyl phosphate as well as β-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.