2种不同方法纯化乳酸杆菌重组S-层融合蛋白的比较试验

将重组菌E.coliBL21（含重组质粒pGEX-SLP）经IPTG诱导获得重组融合蛋白GST-SLP,分别用非特异性的氯化锂沉淀方法和特异性的Pierce（R）GST Spin Purification Kit纯化方法,将该融合蛋白进行纯化,纯化结果采用SDS-PAGE方法进行鉴定.结果显示,2种方法均能够获得大小约为71 ku的目的融合蛋白,但氯化锂沉淀方法纯化效果不及Pierce（R）GST Spin Purification Kit方法.该研究结果为进一步研究乳酸杆菌S-层蛋白生物学特性提供了参考.

Comparison Test of Recombinant S-layer Fusion Protein of Lactobacillus spp.Purified by Two Different Methods

The recombinant E. coli BL21 （containing recombinant plasmid pGEX-SLP）was induced by IPTG to obtain recombinant fusion protein GST-SLP. This fusion protein was purified by non-specific lithium chloride precipitation and specific Pierce GST Spin Purification Kit purification method. The purified results were identified by SDS-PAGE. The results showed that the target fusion protein with the size of about 71 ku could be purified by using two methods, but the purification effect by lithium chloride precipitation method was less than that of Pierce GST Spin Purification Kit purification method. The study results provided references for further research on the biological characteristics of S-layer protein of Lactobacillus spp..