Purification of Nonmitogenic Recombinant Human Acidic Fibroblast Growth Factor in Escherichia coli
Non-mitogenic form ofrecombinant Human acidic fibroblast growthfactor (nrhaFGF) retained the cardio andneuro-protective characters of the wild-typeaFGF while decreased the potential sideeffects like mitogenesis activity. In this paper,nrhaFGF was successfully expressed inEscherichia coli and yielded about 5% of thetotal soluble protein in the 10L fermentationtank. The succeedent chromatography, cationexchange and heparin affinity gained thepurity 55.0% and 95.6% sepecifically, afterdesalting with Sephadex G 25, aggregationwas found increased 2-4% after thelyophilization, and Sephadex G75 completelyeliminated the aggregates whileuntrafiltration with cellulose triacetatemembrane left 2% aggregates in the samples.The chromatography method and the theaggregation removal method with sizeexclusion chromatography were easily scaledup and spade the work for the later clinicaltrials.
Hui YUAN Xiao Kun LI
Zhejiang University of Science and Technology Key Laboratory of Agricultural Products Chemical and B Wenzhou Medical College Bio-natural Pharmaceutiacl School Wenzhou, P.R.China, 325035
国际会议
成都
英文
1-5
2010-06-18（万方平台首次上网日期，不代表论文的发表时间）