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. Author manuscript; available in PMC: 2016 Mar 13.

Published in final edited form as: Biochem Biophys Res Commun. 2015 Feb 13;458(3):626–631. doi: 10.1016/j.bbrc.2015.01.158

(A) Liver cytosolic proteins from PIMT KO mice or ethanol-fed rats were enriched through binding and elution from a MONO Q column. Proteins were stained with colloidal Coomassie (upper panel). The start of elution of the ~160 kDa protein doublet in fraction 7 is marked with an arrowhead. The level of isoaspartate damage in each fraction was quantified (lower panel). (B) Peak column fractions 7-10 were concentrated, fractioned, and then resolved by 1D PAGE. Proteins were stained with colloidal Coomassie, or radiolabelled by PIMT using ³H-SAM, and radiolabelled proteins visualised by autoradiography. Co-distribution of protein staining and isoaspartate radiolabelling was evident for the ~160 kDa protein for both PIMT KO mice and ethanol-fed rats (marked with arrowheads).

(A) Liver cytosolic proteins from PIMT KO mice or ethanol-fed rats were enriched through binding and elution from a MONO Q column. Proteins were stained with colloidal Coomassie (upper panel). The start of elution of the ~160 kDa protein doublet in fraction 7 is marked with an arrowhead. The level of isoaspartate damage in each fraction was quantified (lower panel). (B) Peak column fractions 7-10 were concentrated, fractioned, and then resolved by 1D PAGE. Proteins were stained with colloidal Coomassie, or radiolabelled by PIMT using ³H-SAM, and radiolabelled proteins visualised by autoradiography. Co-distribution of protein staining and isoaspartate radiolabelling was evident for the ~160 kDa protein for both PIMT KO mice and ethanol-fed rats (marked with arrowheads).