Strongyloides ransomi: proteolytic enzymes from larvae.
The filariform larvae of Strongyloides ransomi can infect their hosts by penetration through skin. In this report, homogenates of these organisms were prepared and their proteolytic enzymes examined. Homogenates prepared in 0.2 M citrate, pH 4.0, contain two thiol-dependent proteinases with molecular weights of approximately 32,000 and 28,000. These proteinases have an acidic pH optimum and show substrate preferences and inhibitor susceptibilities similar to the vertebrate acidic cysteinyl proteinases. Homogenates prepared in 0.1 M Tris, pH 7.5, contain multiple proteolytic enzymes, active against both Azocoll and synthetic substrates. These enzymes do not require thiols for activity and they have an alkaline pH optimum. The enzymes are inhibited by both chelating agents and heavy metals, but not by serine-proteinase inhibitors. Extracts prepared in 0.1 M Tris-HCl, pH 7.5, contain endogenous proteinase inhibitors.
D000818:Animals; D003546:Cysteine Endopeptidases; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007814:Larva / Q000201:enzymology; D008666:Metalloendopeptidases; D008970:Molecular Weight; D011480:Protease Inhibitors / Q000494:pharmacology; D013321:Strongyloides / Q000201:enzymology* / Q000254:growth & development; D013379:Substrate Specificity
D011480:Protease Inhibitors; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D008666:Metalloendopeptidases