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High‐molecular‐weight serum proteins from Locusta migratoria: identification of a protein specifically binding juvenile hormone III
Author(s) -
BRUIJN S. M. de,
KOOPMANSCHAP A. B.,
KORT C. A. D. de
Publication year - 1986
Publication title -
physiological entomology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.693
H-Index - 57
eISSN - 1365-3032
pISSN - 0307-6962
DOI - 10.1111/j.1365-3032.1986.tb00385.x
Subject(s) - biology , biochemistry , molecular mass , protein subunit , binding protein , dna binding protein , polyacrylamide gel electrophoresis , gel electrophoresis , hemolymph , microbiology and biotechnology , enzyme , transcription factor , gene
. Tritiated 10,11‐epoxyfarnesyl diazoacetate (EFDA), a photoaffinity label, can be covalently attached to the binding site of a JH‐III‐specific binding protein in the haemolymph of Locusta migratoria migratorioides (R & F). The specificity of the binding of EFDA to the binding protein is verified by displacement with excess unlabelled JH‐III, and EFDA can be used to identify the binding protein in native pore‐limiting gradient poly(acrylamide) gel electrophoresis (PAGE) and sodium dodecyl sulphate‐PAGE. The native binding protein has a molecular weight of 575,000 and is composed of seemingly identical subunits of molecular weight 81,000. Three other high‐molecular weight serum proteins are identified by native PAGE: a lipophorin, composed of two kinds of apolipophorins, a larval storage protein and a cyanoprotein. The molecular weights and subunit structures of these proteins are investigated, but none of these other high‐molecular weight proteins bind JH‐III to an appreciable extent.