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《Xinjiang Agricultural Sciences》 2017-07
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Analysis of the Binding Effect of Follicle Stimulating Hormone Peptide and Different Fragments of Extracellular Domain

ZHAO Ting;XI Ou-yan;QIN Rui-ping;QIU Lin-lin;MA Xiao-lin;LI Jiang-wei;Xinjiang Key Laboratory of Biological Resources and Genetic Engineering/College of Life Science and Technology,Xinjiang University;  
【Objective】The FSH33-53 peptide binds to its receptor FSHR and activates the downstream signal as a FSH functional peptide.However,its specific binding position on the receptor is unclear.The aim of this study is to elucidate the binding region of the FSH33-53 peptide on the receptor FSHR in the hope of providing a basis for FSH-based vaccine design.【Method】The extracellular domain( ECD) and leucine-rich repeat( LRR) of follicle-stimulating hormone receptor was amplified by polymerase chain reaction( PCR) and constructed recombinant plasmids p ET22b-FSHR-ECD and p ET22b-FSHR-LRR.Protein FSHR-ECD and FSHR-LRR were obtained by expression and purification.FSHR9-30-KLH.was obtained by peptide synthesis,and binding and affinity of receptor fragments with FSH33-53 peptide were detected by ELISA method.【Result】The proteins FSHR-ECD and FSHR-LRR were successfully expressed and purified and their relative molecular mass( MR) was 43 and 32 kda.,respectively.When the receptor was 0.5 μg/m L and the ligand was 2.5 μg/m L,the three proteins were bound to the FSH33-53 peptide.The affinity of ELISA to detect the ligand and ligand was 0.21 × 10-6,0.45 × 10-6and 0.056 × 10-6mol/L,respectively.【Conclusion】The binding of LRR fragment to FSH33-53 peptide is stronger than that of the other two fragments.
【Fund】: 国家自然科学基金项目“抗卵泡刺激素受体纳米抗体的制备及其在肿瘤分子显像和抗血管治疗中的作用”(81260333)~~
【CateGory Index】: Q78;R91
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