Abstract:
:This study reports the biochemical characterization and comparative analyses of highly active serine proteases in the larval and pupal developmental stages of Aedes aegypti (Linnaeus) using substrate-SDS-PAGE. Zymographic analysis of larval stadia detected proteolytic activity in 6-8 bands with apparent molecular masses ranging from 20 to 250 kDa, with activity observed from pH 5.5 to 10.0. The pupal stage showed a complex proteolytic activity in at least 11 bands with apparent Mr ranging from 25 to 250 kDa, and pH optimum at 10.0. The proteolytic activities of both larval and pupal stages were strongly inhibited by phenyl-methyl sulfonyl-fluoride and N-α-Tosyl-L-lysine chloromethyl ketone hydrochloride, indicating that the main proteases expressed by these developmental stages are trypsin-like serine proteases. The enzymes were active at temperatures ranging from 4 to 85°C, with optimal activity between 37 and 60°C, and low activity at 85°C. Comparative analysis between the proteolytic enzymes expressed by larvae and pupae showed that substantial changes in the expression of active trypsin-like serine proteases occur during the developmental cycle of A. aegypti.
journal_name
Arch Insect Biochem Physioljournal_title
Archives of insect biochemistry and physiologyauthors
Mesquita-Rodrigues C,Saboia-Vahia L,Cuervo P,Levy CM,Honorio NA,Domont GB,de Jesus JBdoi
10.1002/arch.20412subject
Has Abstractpub_date
2011-04-01 00:00:00pages
223-35issue
4eissn
0739-4462issn
1520-6327journal_volume
76pub_type
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