Please use this identifier to cite or link to this item:
Type
ArticleCopyright
Open access
Collections
- IOC - Artigos de Periódicos [12978]
Metadata
Show full item record
SERINE PROTEASE ACTIVITIES IN OXYSARCODEXIA THORNAX (WALKER) (DIPTERA: SARCOPHAGIDAE) FIRST INSTAR LARVA
Proteases de serina semelhantes a quimotripsina
Oxysarcodexia thornax
Author
Affilliation
Abstract
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 µM), a specific inhibitor of chymotrypsin-like serine proteases.
Keywords in Portuguese
SarcofagídeosProteases de serina semelhantes a quimotripsina
Oxysarcodexia thornax
Share