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Identification and characterization of a novel postlarval hemolymph protein from Manduca sexta
Author(s) -
Ryan Robert O.,
Cole Kenneth D.,
Kawooya John K.,
Wells Michael A.,
Law John H.
Publication year - 1988
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.940090202
Subject(s) - manduca sexta , hemolymph , biology , biochemistry , manduca , immunoprecipitation , sphingidae , gel electrophoresis , methionine , in vivo , microbiology and biotechnology , amino acid , larva , gene , botany
The identification, purification and characterization of a new postlarval specific hemolymph protein from Manduca sexta is described. Incorporation of [ 35 S]methionine into Manduca sexta hemolymph proteins in vivo was investigated as a function of development. A major protein band of M r ≈ 50,000 was highly labeled during the prepupal and adult stage but not in feeding larvae. This postlarval protein (PLP) was isolated from adult male hemolymph and its chemical and immunological properties determined. PLP is a basic protein (pI ∼8.6). Electrophoresis under denaturing conditions reveals a subunit M r ≈ 50,000 while the native protein has an apparent M r ∼ 85,000 by gel permeation chromatography. Anti‐PLP serum recognized PLP but not other hemolymph proteins on immunoblots. In vitro translation of fat body mRNA followed by immunoprecipitation revealed that fat body is the site of PLP synthesis. Quantitation of PLP levels in hemolymph throughout development was performed and suggests PLP may play a role in adult development of M. sexta .