Assay and identification of juvenile hormone binding proteins in leucophaea maderae
Assay and identification of juvenile hormone binding proteins in leucophaea maderae
复制标题
马德拉白蚁保幼激素结合蛋白的测定与鉴定
DOI：
10.1016/0303-7207(83)90154-5
复制
发表时间：
1983
影响因子：
4.1
通讯作者：
J. Koeppe
中科院分区：
文献类型：
--
作者：
G. Kovalick;J. Koeppe
We modified a binding assay using polyethylene glycol (PEG) to precipitate bound hormone. Optimum precipitation occurred when reaction mixtures were incubated with 10–40% PEG and 1.25–2.5 mg/ml γ-globulins for 2–90 min at 4 or 23°C. Results from this assay and from the dextran-coated charcoal assay were similar. Addition of phenylmethylsulfonyl fluoride eliminated nonspecific esterase activity in extracts. JH III-binding macromolecules were identified in hemolymph and ovaries ofLeucophaea maderae. These molecules were pronase- and heat-sensitive and saturable. Using Scatchard analysis an averageKDof 2.04 (±0.32)×l0-8M and 1.91 (±0.80)×10-8M was calculated for hemolymph and ovarian binding proteins. JH III had the highest affinity for binding sites, followed by JH I and JH 0. Various extraction procedures caused changes in JH affinity for both binding proteins. At high concentrations the ( + ) isomer and mixed isomer preparations of methoprene and hydroprene competed for binding sites. Binding proteins had no affinity for the ( − ) isomer or for the JH III acid.
