Analyze the bioactivity of PD-1 and PD-L1 recombination protein which expressed by prokaryotic system
10.3760/cma.j.issn.1003-9279.2009.06.008
- VernacularTitle:原核表达的PD-1与PD-L1融合蛋白相互作用分析
- Author:
Li-Ping SHEN
1
;
Long XU
;
Jian-Dong LI
;
Si-Yong CHEN
;
Yu GUO
;
Feng QIU
;
Sheng-Li BI
Author Information
1. 中国疾病预防控制中心病毒病预防控制所
- Keywords:
Viral fusion proteins;
Membrane protein;
Receptors;
immanosic;
Gene expression regulation;
viral;
Biological assay
- From:
Chinese Journal of Experimental and Clinical Virology
2009;23(6):424-426
- CountryChina
- Language:Chinese
-
Abstract:
Objective To analyze the interaction of PD-1 and PD-L1 recombination protein and to know their bioactivity and affinity.Methods Stick the PD-1 protein on the surface of CM5 isensor chip by the method of Ammine coupling after being preconsentrated.Dilute the PD-L1 protein step by step and reject it to the passage on CM5 sensor chip which had been stick bv PD-1.The time of combination is 3 minutes and of separation is 15 minutes,respectively.Observe the procession and analyze data by BIA Evaluation software 4.Results On the consistency of 40 μg/ml.pH 4.5,the PD-1 protein could couple steady on the surface of CM5senser chip,RU is 3300.On the density of 200 mmol/ml PD-L1 could combine with PD-1 specifically,RU=150,K_D=3.5 × 10~(-6).Conclusion The PD-1 and PD-L1 recombination protein which we expressed by prokaryotic system have good affinity and bioactivity.The results could provide basic condition for later studv.
