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• W2050869101 endingPage "149" @default.
• W2050869101 startingPage "139" @default.
• W2050869101 abstract "The principal digestive proteinases of the gypsy moth, Lymantria dispar, larval midgut were identified, and the subcellular distribution of the enzyme activities was determined. Proteinase activities of fifth-instar larvae were largely attributed to two luminal serine proteinases, a trypsin-like enzyme (TLE) and an elastase 2-like enzyme (ELA). TLE was purified to homegeneity by benzamidine-Sepharose affinity chromatography. With respect to size (Mr = 25 kDa), substrate specificity, and interaction with trypsin inhibitors, the gypsy moth enzyme resembled mammalian pancreatic trypsin and trypsin-like enzymes from other insects. Gypsy moth elastase (ELA) was purified from the benzamidine-Sepharose flow-through by mono-Q FPLC. ELA exhibitied a slightly smaller size (Mr = 24 kDa) than TLE. The insect enzyme was inhibitied by DFP and chymostatin but was unaffected by TPCK. ELA exhibitied little esterolytic activity with BTEE. Succinyl-Ala-Ala-Pro-Leu p-nitroanilide was one of the best substrates for ELA, which is characteristic of elastase 2. TLE and ELA constituted c. 6% of the total soluble protein in midgut lumen of actively feeding fifth-instar larvae. Chymotrypsin and carboxypeptidase activities were not detected in any midgut fraction examined. The brush border membrane (BBM) leucine aminopeptidase (LAP) was isolated from CHAPS-solubilized BBM by FPLC. SDS-PAGE results indicated that the aminopeptidase has an apparent molecular size of c. 100 kDa. The aminopeptidase was inhibited by bestatin and was unaffected by serine proteinase inhibitors." @default.
• W2050869101 created "2016-06-24" @default.
• W2050869101 creator A5068422282 @default.
• W2050869101 date "1995-01-01" @default.
• W2050869101 modified "2023-10-18" @default.
• W2050869101 title "Gypsy moth midgut proteinases: Purification and characterization of luminal trypsin, elastase and the brush border membrane leucine aminopeptidase" @default.
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• W2050869101 doi "https://doi.org/10.1016/0965-1748(94)00033-e" @default.
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