Peptidases of pinworms Syphacia muris and Passalurus ambiguus
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
20433830
DOI
10.1016/j.exppara.2010.04.018
PII: S0014-4894(10)00135-9
Knihovny.cz E-resources
- MeSH
- Edetic Acid pharmacology MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Protease Inhibitors pharmacology MeSH
- Host-Parasite Interactions physiology MeSH
- Hydrogen-Ion Concentration MeSH
- Rabbits MeSH
- Rats MeSH
- Animals, Laboratory MeSH
- Molecular Weight MeSH
- Mucins metabolism MeSH
- Oxyuriasis parasitology MeSH
- Oxyuroidea enzymology MeSH
- Rats, Wistar MeSH
- Peptide Hydrolases chemistry metabolism MeSH
- Substrate Specificity MeSH
- Sulfones pharmacology MeSH
- Gelatin metabolism MeSH
- Animals MeSH
- Check Tag
- Rabbits MeSH
- Rats MeSH
- Male MeSH
- Female MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- 4-(2-aminoethyl)benzenesulfonylfluoride MeSH Browser
- Edetic Acid MeSH
- Protease Inhibitors MeSH
- Mucins MeSH
- Peptide Hydrolases MeSH
- Sulfones MeSH
- Gelatin MeSH
In this first report about pinworms peptidases we primarily characterize peptidases released during in vitro maintenance of two common pinworms of laboratory animals -Syphacia muris and Passalurus ambiguus. The peptidase activity obtained using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) showed the presence of peptidases from S. muris with a wide range of molecular size (25-110 kDa), which degrades gelatin and mucin at alkaline pH levels. P. ambiguus released serine and aspartyl peptidases degrading gelatin at all tested pH (3, 5, 7, and 9) and at acidic pH Passalurus released aspartyl and cysteine peptidases which are active against mucin.
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