کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1206640 | 965242 | 2009 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Efficient purification of recombinant proteins fused to maltose-binding protein by mixed-mode chromatography Efficient purification of recombinant proteins fused to maltose-binding protein by mixed-mode chromatography](/preview/png/1206640.png)
Two mixed-mode resins were evaluated as an alternative to conventional affinity resins for the purification of recombinant proteins fused to maltose-binding protein (MPB). We purified recombinant MBP, MBP-LacZ and MBP-Leap2 from crude Escherichia coli extracts. Mixed-mode resins allowed the efficient purification of MBP-fused proteins. Indeed, the quantity of purified proteins was significantly higher with mixed-mode resins, and their purity was equivalent to that obtained with affinity resins. By using purified MBP, MBP-LacZ and MBP-Leap2, the dynamic binding capacity of mixed-mode resins was 5-fold higher than that of affinity resins. Moreover, the recovery for the three proteins studied was in the 50–60% range for affinity resins, and in the 80–85% range for mixed-mode resins. Mixed-mode resins thus represent a powerful alternative to the classical amylose or dextrin resins for the purification of recombinant proteins fused to maltose-binding protein.
Journal: Journal of Chromatography A - Volume 1216, Issue 20, 15 May 2009, Pages 4451–4456