Peptidases from Plasmodium falciparum cultured in vitro.
An acid peptidase that degrades hemoglobin optimally at pH 3.5, a neutral aminopeptidase and an alkaline endopeptidase that acts on an alpha-N-blocked synthetic substrate have been demonstrated in Plasmodium falciparum in culture. The enzymes were shown to be distinct by anion exchange chromatography, gel filtration on Sephadex G-200 and isoelectric focusing. The activities of the acid peptidase and the aminopeptidase were inhibited by antimalarial compounds.
D000818:Animals; D000962:Antimalarials / Q000494:pharmacology; D002848:Chromatography, DEAE-Cellulose; D003470:Culture Media; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000145:classification / Q000378:metabolism*; D010963:Plasmodium falciparum / Q000201:enzymology*
D000962:Antimalarials; D003470:Culture Media; D010447:Peptide Hydrolases