从四龄烟草天蛾（Manduca sexta）血淋巴中纯化和鉴定一种保幼激素结合蛋白
Purification and characterization of a juvenile hormone binding protein from the hemolymph of the fourth instar tobacco hornworm, Manduca sexta.
作者信息
Goodman W, O'Hern P A, Zaugg R H, Gilbert L I
出版信息
Mol Cell Endocrinol. 1978 Jul-Aug;11(2):225-42. doi: 10.1016/0303-7207(78)90010-2.
A protein which binds the insect juvenile hormone has been isolated from the hemolymph of the fourth instar tobacco hornworm, Manduca sexta (Lepidoptera). Bioassay and chemical characterization of the bound ligand from the purified binding protein indicates that this molecule is the primary macromolecule responsible for juvenile hormone transport in the hemolymph of this insect. The juvenile hormone binding protein has been purified using gel filtration, ion exchange chromatography and preparative polyacrylamide gel electrophoresis. The protein is a single polypeptide chain of about 28,000 daltons with a sedimentation coefficient of 2.2S and an isoelectric point of 5.0. Binding analysis using a hydroxyapatite batch assay indicates that the juvenile hormone binding protein has one binding site with a Ka of 1.2 times 10(7) M-1 at 4 degrees C.
一种与昆虫保幼激素结合的蛋白质已从四龄烟草天蛾（烟草天蛾，鳞翅目）的血淋巴中分离出来。对纯化的结合蛋白所结合配体的生物测定和化学表征表明，该分子是负责这种昆虫血淋巴中保幼激素运输的主要大分子。保幼激素结合蛋白已通过凝胶过滤、离子交换色谱和制备性聚丙烯酰胺凝胶电泳进行了纯化。该蛋白是一条约28,000道尔顿的单多肽链，沉降系数为2.2S，等电点为5.0。使用羟基磷灰石批量分析法进行的结合分析表明，保幼激素结合蛋白在4℃时有一个结合位点，其解离常数Ka为1.2×10⁷ M⁻¹。
Zotero 插件