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Title:Cuticular Proteins of Hyalophora Cecropia: Characterization With Electrophoresis, Antibodies, and Lectins (Insect, Hydrophogicity, Metamorphosis, Glycoproteins, Avidin-Biotin)
Author(s):Cox, Diana Lynn
Department / Program:Entomology
Degree Granting Institution:University of Illinois at Urbana-Champaign
Subject(s):Biology, Entomology
Abstract:The soluble cuticular proteins of defined anatomical regions from different metamorphic stages of the giant silkmoth, Hyalophora cecropia, were characterized by electrophoresis and by reactions with antibodies and lectins. As urea concentration in 2D gels was increased, some of the cuticular proteins from the larval dorsal abdomen decreased in mobility relative to the molecular weight standards. This decrease was found to be dependent on the pH and ionic strength of the resolving gel. This behavior has been interpreted as reflecting the extreme hydrophobic and globular nature of many cuticular proteins. Evidence for different multigene families of cuticular proteins was indicated by similar behavior of groups of proteins under different electrophoretic conditions. Common families were found in cuticles with similar flexibilities from different metamorphic stages, yet there was evidence that different members of a single family were independently regulated. Glycosylated proteins were visualized by Periodic Acid-Schiff staining and also on Western Blots of IEF and 2D gels with biotinylated lectins and the avidin-biotin-complex method. More cuticular proteins from flexible cuticular regions than from rigid cuticles were glycosylated, but in both cases these were minor proteins as detected by Coomassie Blue. These proteins contained primarily N-acetyl-galactosamine and mannose. Low levels of N-acetyl-glucosamine, galactose, and fucose were detected in a few minor proteins. No sialic acid was detected using either lectins or neuraminidase digestion. On Western Blots, it was the glycosylated proteins which were most antigenic, suggesting that antibodies had been made against the carbohydrate moieties. Gels of proteins from cuticular regions with similar flexibility had more spots in common, and the individual proteins were more antigenically alike and had similar types and levels of glycosylation.
Issue Date:1985
Description:146 p.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1985.
Other Identifier(s):(UMI)AAI8600157
Date Available in IDEALS:2014-12-16
Date Deposited:1985

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