Serine protease activities in Oxysarcodexia thornax (Walker) (Diptera: Sarcophagidae) first instar larva.
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.
Cuervo
Patrícia
P
Laboratório de Pesquisas em Leishmanioses, Instituto Oswaldo Cruz, Fiocruz, Rio de Janeiro, Brasil.
Mesquita-Rodrigues
Camila
C
d'Avila Levy
Claudia Masini
CM
Britto
Constança
C
Pires
Fabiano Araújo
FA
Gredilha
Rodrigo
R
Alves
Carlos Roberto
CR
Jesus
Jose Batista de
JB
D000818:Animals; D004175:Diptera / Q000201:enzymology* / Q000254:growth & development; D004591:Electrophoresis, Polyacrylamide Gel; D007814:Larva / Q000201:enzymology; D012697:Serine Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*
D012697:Serine Endopeptidases