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Characterization of midgut proteinase activities of white grubs: Lepidiota noxia, Lepidiota negatoria , and Antitrogus consanguineus (scarabaeidae, melolonthini)
Author(s) -
McGhie Tony K.,
Christeller John T.,
Ford Rebecca,
Allsopp Peter G.
Publication year - 1995
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.940280405
Subject(s) - biology , elastase , chymotrypsin , trypsin , serine proteinase inhibitors , aminopeptidase , biochemistry , serine , midgut , cysteine , pancreatic elastase , leucine , enzyme , leucyl aminopeptidase , amino acid , larva , serine protease , protease , botany
The proteinases in the midguts of three scarab white grub species, Lepidiota noxia, L. negatoria , and Antitrogus consanguineus , were investigated to classify the proteinases present and to determine the most effective proteinase inhibitor for potential use as an insect control agent. pH activity profiles indicated the presence of serine proteinases and the absence of cysteine proteinases. This was confirmed by the lack of inhibition by specific cysteine proteinase inhibitors. Trypsin, chymotrypsin, elastase, and leucine aminopeptidase activities were detected by using specific synthetic substrates. A screen of 32 proteinase inhibitors produced 9 inhibitors of trypsin, chymotrypsin, and elastase which reduced proteolytic activity by greater than 75%. © 1995 Wiley‐Liss, Inc.