Acid phosphatase activity demonstrated by intact Angiostrongylus cantonesis with special reference to its function.
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.
D000135:Acid Phosphatase / Q000378:metabolism*; D000818:Animals; D005260:Female; D005947:Glucose / Q000378:metabolism; D005958:Glucosephosphates / Q000378:metabolism; D005994:Glycerophosphates / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007773:Lactates / Q000096:biosynthesis; D008681:Metastrongyloidea / Q000201:enzymology*; D008982:Molybdenum / Q000494:pharmacology; D009349:Nematode Infections / Q000469:parasitology; D009596:Nitrophenols / Q000378:metabolism; D009711:Nucleotides / Q000378:metabolism; D009943:Organophosphorus Compounds / Q000378:metabolism; D051381:Rats; D013379:Substrate Specificity
D005958:Glucosephosphates; D005994:Glycerophosphates; D007773:Lactates; D009596:Nitrophenols; D009711:Nucleotides; D009943:Organophosphorus Compounds; C008644:nitrophenylphosphate; D008982:Molybdenum; D000135:Acid Phosphatase; D005947:Glucose