A NOVEL USE FOR COOMASSIE BRILLIANT BLUE (R-250) IN PROTEIN GEL-DRYING PROCEDURE AND ASSESSING THE ELECTRO-TRANSFERRING EFFICIENCY

The present study provides an alternative method for protein-gel dryin g. Rat brain protein extracts were separated using sodium dodecyl sulf ate-polyacrylamide gel electrophoresis (SDS-PAGE) followed by staining with coomassie brilliant blue (R-250). The stained gel was then subje cted to electroblotting on nitrocellulose membranes. This method exhib ited four advantages: 1) it eliminated problems associated with gel-dr ying (e.g., shrinkage of gel), 2) it allowed assessment of the efficie ncy of electro-transfer, 3) it significantly reduced the time of gel-d rying procedure by an average of 40 minutes and 4) it facilitated visu alizing electro-transferred proteins with the same efficiency as the c ommon amidoblack staining technique. In conclusion, the described meth od is simple, economical and introduces several applications. (C) 1996 Academic Press, Inc.