Serine protease activities in Oxysarcodexia thornax (Walker) (Diptera: Sarcophagidae) first instar larva
| Autor: | Claudia Masini d’Avila Levy, Carlos Roberto Alves, Camila Mesquita-Rodrigues, Patricia Cuervo, Rodrigo Gredilha, Jose Batista de Jesus, F.A. Pires, Constança Britto |
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| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
Microbiology (medical)
Proteases lcsh:Arctic medicine. Tropical medicine lcsh:RC955-962 medicine.medical_treatment Sarcophagidae lcsh:QR1-502 Biology chymotrypsin-like serine proteases lcsh:Microbiology Serine medicine Animals Polyacrylamide gel electrophoresis chemistry.chemical_classification Serine protease Larva Protease Flesh fly Diptera Serine Endopeptidases fungi biology.organism_classification Molecular biology Oxysarcodexia thornax Enzyme chemistry Biochemistry biology.protein Electrophoresis Polyacrylamide Gel |
| Zdroj: | Memórias do Instituto Oswaldo Cruz., Vol 103, Iss 5, Pp 504-506 (2008) Memórias do Instituto Oswaldo Cruz, Volume: 103, Issue: 5, Pages: 504-506, Published: AUG 2008 |
| ISSN: | 1678-8060 0074-0276 |
| Popis: | We report for the first time the expression of multiple protease activities in the first instar larva (L1) of the flesh fly Oxysarcodexia thornax (Walker). Zymographic analysis of homogenates from freshly obtained L1 revealed a complex proteolytic profile ranging from 21.5 to 136 kDa. Although some activities were detected at pH 3.5 and 5.5, the optimum pH for most of the proteolytic activities was between pH 7.5 and 9.5. Seven of 10 proteases were completely inactivated by phenyl-methyl sulfonyl-fluoride, suggesting that main proteases expressed by L1 belong to serine proteases class. Complete inactivation of all enzymatic activities was obtained using N-p-Tosyl-L-phenylalanine chloromethyl ketone (100 microM), a specific inhibitor of chymotrypsin-like serine proteases. |
| Databáze: | OpenAIRE |
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