Neutral protease activities at different developmental stages of Schistosoma mansoni in mammalian hosts.
Neutral protease activities of schistosomula, 20 day old and adult worms of S. mansoni have been studied. 1. The neutral enzymes of the three development stages are able to hydrolyse numerous natural and synthetic substrates. 2. The enzymes of homogenates and saponin CaC12 extracts show significant discrepancies in their specificities, optimum pH activities and in the effects of enzyme inhibitors. 3. A serine protease activity was specific for the schistosomula stage whereas thiol proteinases characterize the later stages of evolution. A metalloaminopeptidase activity was shown at all three stages. 4. Gel filtration chromatography and isoelectric focusing of an adult worm homogenate demonstrated the presence of at least 5 caseolytic and 4 azocollytic neutral activities. Three aminopeptidases, one of which exhibited iminopeptidase specificity were revealed by the same procedure.
D000626:Aminopeptidases / Q000378:metabolism; D000818:Animals; D006224:Cricetinae; D010450:Endopeptidases / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D010447:Peptide Hydrolases / Q000378:metabolism*; D012550:Schistosoma mansoni / Q000201:enzymology* / Q000254:growth & development; D012552:Schistosomiasis / Q000469:parasitology*; D012697:Serine Endopeptidases; D014020:Tissue Extracts / Q000378:metabolism
D014020:Tissue Extracts; D010450:Endopeptidases; D010447:Peptide Hydrolases; D000626:Aminopeptidases; D012697:Serine Endopeptidases