Additional file 3.

Figure S2.Purification of LPCAT1, C211T and Cys12- protein. Proteins were produced in E. coli and extracted from the membrane in presence of 2% CHAPS. Then, CHAPS concentration was decreased to 1%, and proteins were applied to a Nickel-Sepharose column. After washing of un-bound proteins, hexa-Histidine tagged LPCAT1 and mutant forms were eluted with imidazole concentration of 50, 200 and 500 mM, as indicated. Ten μl of samples were loaded of 12% SDS-PAGE gel and after separation by electrophoresis, proteins were stained with coomassie blue. Note that all three forms were partially pure (indicated by an asterisk) in the fraction eluted by 500 mM imidazole. Molecular mass standard is shown of the right side of the gels.

Format: PDF Size: 2.4MB Download file

This file can be viewed with: Adobe Acrobat Reader

Soupene and Kuypers BMC Biochemistry 2012 13:8   doi:10.1186/1471-2091-13-8