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Basic isoforms of hemolymph storage proteins expressed during larval metamorphosis
Author(s) -
Jones Grace,
Sarkari Neville
Publication year - 1993
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.940240106
Subject(s) - hemolymph , biology , juvenile hormone , metamorphosis , trichoplusia , hemocyanin , storage protein , antiserum , gene isoform , instar , larva , biochemistry , juvenile , microbiology and biotechnology , hormone , botany , antibody , genetics , gene , noctuidae
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, 150,000) was identified that cross‐reacted specifically with an antiserum raised against a normally basic, M 74,000 juvenile hormone suppressible protein in the hemocyanin superfamily. © 1993 Wiley‐Liss, Inc.