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2009年01月13日
【期刊论文】Expression, refolding, and characterization of a novel recombinant dual human stem cell factor
秦浚川， Haiqin Lu， Yuhui Zang， Yuguan Ze， Jie Zhu， Tao Chen， Junhai Han， Junchuan Qin*
Protein Expression and PuriWcation 43(2005)126-132，-0001，（）：
-1年11月30日
A novel recombinant dual human stem cell factor (rdhSCF) gene which consisted of a full-length hSCF(1-165 aa) cDNA and atruncated hSCF (1-145 aa) cDNA, linked by a peptide (GGGGSGGGGSGG) coding region, was constructed and cloned into Escherichia coli expression vector pET-22b. The rdhSCF was expressed at high level in E. coli BL21(DE3) and existed mainly as inclusion bodies. The inclusion bodies were solubilized in urea and refolded by ion-exchange chromatography. After renaturation, the purity of the yielded rdhSCF was up to 90%. Cell proliferation assay showed that the speciWc activity of the rdhSCF was 2.86
Dual human stem cell factor， pET-22b， Refolding， Escherichia coli expression system， BL21(， DE3)，
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2009年01月13日
秦浚川， Haiqin Lu， Jie Zhu， Yuhui Zang， Yuguan Ze， Junchuan Qin*
Biochemical Pharmacology 70(2005)1019-1025，-0001，（）：
-1年11月30日
Human paraoxnase-3 (hPON3) (EC3.1.8.1) is a lipid-associated enzyme with antioxidant activity, and can inhibit the oxidation of lowdensity lipoprotein (LDL), thereby inhibiting early atherogenic process. In the present study, human PON3 gene was cloned from Human Fetal Liver Marathon-Ready cDNA and expressed in insect cells using baculovirus vector. Twenty-eight milligrams of purified recombinant hPON3 (rhPON3) was obtained from 1 L Sf9 cells culture. The Km and Vmax values of rhPON3, with respective to phenylacetate hydrolysis were 7.46
Human paraoxonase-3， Baculovirus-mediated expression system， Sf9 cell， Gene expression， LDL oxidation， Dihydrocoumarin
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