3.1.3.7	-	729266, 81106, 81107, 81108	
3.1.3.7	adenosine 3',5'-bisphosphate-agarose resin column chromatography	696267	
3.1.3.7	aqueous two-phase micellar system (ATPMS), as an alternative liquid-liquid extraction technique, is exploited for the precise separation or large-scale concentration of biomolecules. An affinity-based ATPMS composed of mixed micelles is constructed by introducing a copper-chelated Triton X-114 (TX-Cu(II)) into an aqueous solution of hydrophobically modified ethylene oxide polymer (HMEO). The phase diagram of the HM-EO/TX-Cu(II) system is measured, and the partitioning behavior of model proteins (YND, BSA, lysozyme) is studied by using this system. The addition of HM-EO can result in formation of the micellar network in the micelle-rich phase, making the phase separation easier and stabler. In addition, the extractive performance of ATPMS is enhanced due to the existence of the mixed micelles composed by HM-EO and Cu(II)-chelated TX. The recombinant His6-tagged enzyme YND from Escherichia coli strain BL21(DE3) is selectively extracted into the micelle-rich phase, while the histidine-poor proteins (BSA and lysozyme) remain in the micelle-poor phase. Enzyme YND can be recovered from the cell lysate with a recovery yield of 49.23% and purification factor of 2.63, method, overview. And purification of the His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography	751193	
3.1.3.7	Ni-NTA column chromatography	677833	
3.1.3.7	nickel affinity chromatography	677661	
3.1.3.7	partial, copurification with other enzymes	81102	
3.1.3.7	recombinant enzyme	651264, 651657, 652120	
3.1.3.7	recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration	749901	
3.1.3.7	recombinant protein	730884	
3.1.3.7	TALON metal affinity resin column chromatography	677696