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Properties of larval and imaginal membrane‐bound digestive enzymes from Trichosia pubescens
Author(s) -
EspinozaFuentes Fernando P.,
Terra Walter R.
Publication year - 1986
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.940030208
Subject(s) - midgut , aminopeptidase , trehalase , tris , biology , enzyme , biochemistry , microbiology and biotechnology , antiserum , larva , leucine , amino acid , antibody , botany , immunology
Abstract Trichosia pubescens larval midgut ceca cells display in their plasma membranes α‐glucosidases (M r 95,000; pH o 5.5; K m 5.7 mM; K i for TRIS 8.9 mM), trehalases (M r 69,000; pH o 5.3; K m 0.92 mM; K i for TRIS 57 mM), and aminopeptidases (M r 95,000; pH o 8.7; K m 0.19 mM) which are solubilized by Triton X‐100. The enzymes were purified by electrophoresis and used to raise antibodies in a rabbit. T. pubescens imaginal midgut cells display in their plasma membranes an α‐glucosidase (M r 156,000; pH o 5.8; K m 2.3 mM; K i for TRIS 0.2 mM), a trehalase (M r 93,000; pH o 5.5; K m 0.72 mM; K i for TRIS 45.5 mM), and an aminopeptidase (M r 210,000; pH o 9.0; K m 0.47 mM). Antiserum produced against the larval enzymes shows no precipitation arc when tested by double immunodiffusion or by immunoelectrophoresis with Triton X‐100‐solubilized membrane proteins from imaginal midguts. Otherwise, a similar test showed that larval midgut cecal enzymes and larval ventriculus enzymes display complete immunological identity. The data suggest that, despite the fact the larval and imaginal aminopeptidase, α‐glucosidase, and trehalase probably have similar functions, the genes coding for them in larvae and imagoes must differ.