摘要
利用糖蛋白4(PRG4)分子多态性的特点,克隆表达含有两个人促细胞生成素B(SMB)结构域及少量糖基化重复序列的重组蛋白(SMBPRG4),并建立了成熟的纯化工艺流程,可高效表达重组蛋白。进一步通过凝胶排阻、动态光散射实验发现重组蛋白具有自我聚集的特点,在溶液中以稳定的二聚体形式存在。结构预测及非还原电泳揭示SMBPRG4是非共价结合的同源二聚体。
Recombinant protein SMBPRG4 containing two Somatomedin B domains and a small amount of glycosylation of repetitive sequences of proteoglycan 4 was cloned according to PGR4 gene polymorphism. Mature purification process was established and recombinant protein SMBPRG4 , with high-level expression was purified. By using size ex- clusion chromatogaraphy and dynamic light scattering, we found that the recombinant protein self-aggregate to di- meric form. Structure prediction and non reducing electrophoresis revealed that SMBPRG4 was a non-covalently bonded dimer.
出处
《生物医学工程学杂志》
EI
CAS
CSCD
北大核心
2014年第6期1319-1324,共6页
Journal of Biomedical Engineering
基金
浙江省卫生高层次创新人才培养工程资助项目
浙江省自然科学基金资助项目(LQ12H16001)
关键词
糖蛋白4
基因表达
结构
蛋白聚集
proteoglyean 4
gene expression
structure
protein aggregation