Photoaffinity labeling and characterization of a juvenile hormone binding protein in the membranes of follicle cells of Locusta migratoria
作者： Veeresh L. Sevala , K.G. Davey , Glenn D. Prestwich
DOI: 10.1016/0965-1748(94)00065-P
关键词: Biology 、 Methoprene 、 Juvenile hormone 、 Binding site 、 Cell surface receptor 、 Biological activity 、 Ligand (biochemistry) 、 Biochemistry 、 Peptide 、 Photoaffinity labeling 、 Molecular biology
摘要: Membrane preparations from vitellogenic follicles of Locusta migratoria incubated with tritium-labeled photoaffinity analogs juvenile hormones and methoprene in the presence or absence excess unlabeled hormone were irradiated, subsequently solubilized, peptides separated by SDS-PAGE radioactive proteins visualized fluorography. Both [3H] epoxyhomofarnesyl diazoacetate ([3H]EHDA), analog JH II, epoxyfarnesyl ([3H]EFDA), III, covalently modified a 35 kDa peptide, this labeling was displaced an II III respectively. No 1-displaceable epoxybishomofarnesyl ([3H]EBDA), I, detected. ([3H]MDK), methoprene, exhibited specific binding to 17 protein. Using (10R)-[3H]JH as ligand, membrane demonstrated possess saturable binding: Scatchard analysis revealed single site Kp 3.68 ± 0.46 nM total capacity (Bmax) 0.375 0.07 pmol per mg The ability various JHs bind reflects previous findings concerning their biological activity on follicle cells vitro, suggesting that is receptor for III.
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