Evidence for a Ca2+-dependent activator protein in the rat tapeworm Hymenolepis diminuta.
A low molecular weight, acidic, heat stable protein has been characterised from the rat tapeworm Hymenolepis diminuta. This protein was found to activate cyclic 3', 5'-nucleotide phosphodiesterase in a Ca2+-dependent manner. The activation process was inhibited by the phenothiazine drug trifluoperazine. The biochemical properties of this protein clearly resemble those of ovine brain calmodulin. Our investigation thus concludes that there is a calmodulin-like activator protein in this cestode.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002147:Calmodulin / Q000032:analysis / Q000302:isolation & purification* / Q000494:pharmacology; D004789:Enzyme Activation; D006926:Hymenolepis / Q000032:analysis*; D008297:Male; D010727:Phosphoric Diester Hydrolases / Q000032:analysis; D051381:Rats; D011919:Rats, Inbred Strains
D000596:Amino Acids; D002147:Calmodulin; D010727:Phosphoric Diester Hydrolases