Purification and characterization of a juvenile hormone binding protein from hemolymph of the silkworm,Bombyx mori |
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| Affiliation: | 1. Carrera Bioquímica, Departamento de Ciencias Químicas y Recursos Naturales, Universidad de La Frontera, Temuco, Chile;2. Laboratorio de Química Ecológica, Departamento de Ciencias Químicas y Recursos Naturales, Universidad de La Frontera, Temuco, Chile;3. Instituto de Ciencias Biológicas, Universidad de Talca, Talca, Chile;4. Millennium Nucleus Centre in Molecular Ecology and Evolutionary Applications in the Agroecosystems, Universidad de Talca, Talca, Chile;5. Centro de Investigación Biotecnológica Aplicada al Medio Ambiente, CIBAMA, Universidad de La Frontera, Temuco, Chile;6. Laboratorio de Ecología Química, Centro Tecnológico de Control Biológico, Instituto de Investigaciones Agropecuarias (INIA)-Quilamapu, Chillán, Chile;1. State Key Laboratory of Environmental and Biological Analysis, Department of Chemistry, Hong Kong Baptist University, Hong Kong SAR, China;2. Institute of Environmental Science, Shanxi University, Taiyuan 030006, China;3. School of Environmental Science and Engineering, Guangdong University of Technology, Guangzhou 510006, China;1. State Key Laboratory of Environmental and Biological Analysis, Department of Chemistry, Hong Kong Baptist University, Hong Kong SAR, China;2. State Key Laboratory of Cotton Biology, Key Laboratory of Plant Stress Biology, School of Life Sciences, Henan University, Kaifeng, China;3. Shandong Analysis and Test Center, Qilu University of Technology (Shandong Academy of Sciences), Jinan, Shandong, China;4. School of Pharmaceutical Sciences (Shenzhen), Sun Yat-Sen University, Shenzhen, China |
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| Abstract: | A juvenile hormone binding protein (JHBP) has been isolated from Bombyx mori hemolymph by gel filtration, ion-exchange chromatography, chromatofocusing and hydroxyapatite column chromatography. Gel electrophoresis indicates that the isolated protein is homogeneous in the presence or absence of a denaturing agent. The JHBP in question has a relative molecular mass of 32 kDa, determined by denaturing gel electrophoresis. Chromatofocusing analysis indicated that the JHBP is an acidic protein with pI 4.9. The protein exhibits a dissociation constant of 9.0 × 10−8 M for JH I, 1.14 × 10−7 M for JH II and 3.9 × 10−7 M for JH III, and thus its affinity for JH analogues is in the order of JHI >JHII >JHIII. Its amino acid composition indicates that the protein consists of 297 residues of 18 kinds of amino acids. The sequence of the N-terminus of the polypeptide chain was determined for 34 of the first 36 residues: Asp-Gln-Asp-Ala-Leu-Leu-Lys-Pro-?-Lys-Leu-Gly-Asp-Met-Gln-Ser-Leu-Ser-Ser-Ala-Thr-Gln-Gln-Phe-Leu-Glu- Lys-Thr-Ser-Lys-Gly-Ile-Pro-?-Tyr-His-. |
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