摘要
以保护鸡胚成纤维细胞(CEF)抵御新城疫病毒(NDV)侵袭的能力为主要检测指标,考察鸡干扰素γ(c-IFNγ)的热稳定性、酸碱稳定性及冻融耐受性。在37℃及以上的热处理中,c-IFNγ样品迅速失活,其中60℃处理1 h活性即降低约70﹪;酸性环境中的样品极不稳定,在pH=2的液体制剂中1 h,蛋白质全部失活,但在碱性制剂中,96 h内其生物活性未发生明显变化;c-IFNγ液体制剂对冻融极为敏感,其生物学活性随冻融次数的增加呈线性下降。鸡干扰素γ重组蛋白对热及酸性环境不稳定,且不易冻存冻融。
Selecting the protecting ability of resisting NDV for chicken embryo fibroblasts as the main indicator, it is studied the thermal stability, pH stability and freeze-thaw tolerance of c-IFNγ. The c-IFNγ, loses its activity rapidly in the heat treatment of 37℃ or above, and the activity can be reduced to 70 % at 60℃ for an hour. The protein which is extremely unstable in acidic environment can lose all of its activity in the liquid preparations of pH = 2 for an hour, but it has no notable change in alkaline environment within 96 hours. The liquid c-IFNγ preparations are very sensitive to the freeze-thaw, whose activity declined linearly with the increase of freeze-thaw. Chicken IFN-γ recombinant proteins, which are not suitable for freezing and thawing, are unstable in heat and acidic environment.
出处
《天津农学院学报》
CAS
2011年第4期9-12,共4页
Journal of Tianjin Agricultural University
基金
天津市科技攻关培育计划项目"鸡重组干扰素γ(IFNγ)的中试"(05YFGPNC01900)
天津市科技计划支撑重点项目"鸡重组干扰素γ生产工艺的优化及产品稳定性研究"(09ZCKFNC00200)
关键词
鸡干扰素γ重组蛋白
热稳定性
酸碱稳定性
冻融耐受性
生物活性
c-IFNγ recombinant proteins
thermal stability
pH stability
freeze-thaw tolerance
biological activity
