Aminopeptidase of Eimeria nieschulzi physico-chemical properties and action of antimalarial drugs.
An aminopeptidase capable of degrading synthetic substrates and short peptides has been demonstrated in Eimeria nieschulzi sporulated oocysts. Physico-chemical properties and the classic activator and inhibitory effects have been determined. The inhibitory activity of classic antimalarial drugs has been demonstrated and the study of the inhibitory mechanism by Chloroquine has been further studied. Lastly, the comparison between the aminopeptidase of Eimeria genus parasites and that of Plasmodium has been discussed.
D000626:Aminopeptidases / Q000378:metabolism*; D000818:Animals; D000962:Antimalarials / Q000494:pharmacology*; D002413:Cations, Divalent / Q000494:pharmacology; D002738:Chloroquine / Q000494:pharmacology*; D004539:Eimeria / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011319:Primaquine / Q000494:pharmacology; D011796:Quinacrine / Q000494:pharmacology; D013696:Temperature
D000962:Antimalarials; D002413:Cations, Divalent; D002738:Chloroquine; D000626:Aminopeptidases; D011796:Quinacrine; D011319:Primaquine