Glutathione activation of a cysteine proteinase from Schistosoma mansoni.
A cysteine proteinase isolated from Schistosoma mansoni adults requires reduction by thiols for activation. The proteinase is located in the parasite digestive tract where it degrades hemoglobin released from host red blood cells. Reduced glutathione (GSH) has been shown to be effective in activation. Total glutathione concentration and the GSH/oxidized glutathione (GSSG) ratio were measured in whole blood lysate (3.2 mM, 284), serum (24 microM, 9.8) and material collected from the parasite digestive tract (4.2 mM, 137). The ratio of GSH/GSSG at which the enzyme displays half-maximal activity (Kox) is 1.0. Proteinase activation as a function of glutathione concentration and time was determined. The first-order reaction yielded a half-time of activation of 13 min at 5 mM. The second-order rate constant was 12.7 M-1 X min-1. The function of the proteinase and its possible regulation by glutathione activation are discussed.
D000818:Animals; D003546:Cysteine Endopeptidases; D010450:Endopeptidases / Q000032:analysis / Q000378:metabolism*; D004789:Enzyme Activation; D005978:Glutathione / Q000502:physiology*; D008970:Molecular Weight; D010084:Oxidation-Reduction; D012550:Schistosoma mansoni / Q000201:enzymology*; D012555:Schistosomiasis mansoni / Q000201:enzymology*; D013997:Time Factors
D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D005978:Glutathione