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• W2048814302 abstract "The major proteases of the grass grub (Costelytra zealandica) larval midgut have been identified, partially purified and characterized. Identification was made initially on the basis of hydrolysis of synthetic substrates (blocked and partially blocked esters and amides of specific amino acids), thus classifying the activities into different classes of endo- and exopeptidases. A range of inhibitors specific to different classes of proteases were used to confirm the presence of trypsin, chymotrypsin, elastase, leucine aminopeptidase and carboxypeptidases A and B and to establish the absence of thiol- and metallo-endopeptidases. The dominant endopeptidase in the midgut is trypsin, which is present in four forms, distinguishable by net charge, but indistinguishable either in terms of Michaelis-Menten parameters (Km and kcat) or in molecular weight (23,000). The pH optimum lies between pH 9–10. Leucine aminopeptidase has a molecular weight of 91,000 and a pH optimum at pH 8.0. Carboxypeptidase A has a molecular weight of 43,000 and a pH optimum at pH 8.5. All enzymes retained substantial activity at pH 7.0–7.1, the pH of the midgut lumen, where the bulk of the activity was located. Protease levels in the hindgut (or fermentation sac) were 1–5% of those in the midgut. The range of enzymes appears sufficient for complete breakdown of ingested protein." @default.
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• W2048814302 date "1989-01-01" @default.
• W2048814302 modified "2023-10-18" @default.
• W2048814302 title "Partial purification and characterization of the major midgut proteases of grass grub larvae (Costelytra zealandica, Coleoptera: Scarabaeidae)" @default.
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• W2048814302 doi "https://doi.org/10.1016/0020-1790(89)90066-8" @default.
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