Basic isoforms of hemolymph storage proteins expressed during larval metamorphosis.
The hemolymph of metamorphosing, final instar larvae of Trichoplusia ni was analyzed for the presence of basic forms of normally positively charged storage proteins. Basic forms of arylphorin and a normally acidic juvenile hormone suppressible protein were identified. For each of these two proteins, variation was observed in the immunoreactivity of forms with different basic charges, where the antisera had been generated against acidic forms of each protein. A basic protein of high molecular size (ca. M(r) 150,000) was identified that cross-reacted specifically with an antiserum raised against a normally basic, M(r) 74,000 juvenile hormone suppressible protein in the hemocyanin superfamily.
School of Biological Sciences, University of Kentucky, Lexington 40506.
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Jones
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Sarkari
D000818:Animals; D000941:Antigens / Q000737:chemistry / Q000302:isolation & purification; D003429:Cross Reactions; D006023:Glycoproteins; D006458:Hemolymph / Q000737:chemistry*; D007120:Immunochemistry; D007301:Insect Hormones / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*; D019476:Insect Proteins; D007814:Larva / Q000737:chemistry; D008675:Metamorphosis, Biological; D008970:Molecular Weight; D009036:Moths / Q000737:chemistry* / Q000254:growth & development
D000941:Antigens; D006023:Glycoproteins; D007301:Insect Hormones; D019476:Insect Proteins; C041137:storage proteins, Insecta