A novel use for coomassie brilliant blue (R250) in protein gel-drying procedure and assessing the electro-transferring efficiency.
The present study provides an alternative method for protein-gel drying. Rat brain protein extracts were separated using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) followed by staining with coomassie brilliant blue (R-250). The stained gel was then subjected to electroblotting on nitrocellulose membranes. This method exhibited four advantages: 1 ) it eliminated problems associated with gel-drying (e.g., ,shrinkage of gel), 2) it allowed assessment of the efficiency of electro-transfer, 3) it significantly reduced the time of gel-drying procedure by an average of 40 minutes and 4) it facilitated visualizing electro-transferred proteins with the same efficiency as the common amidoblack staining technique. In conclusion, the described method is simple, economical and introduces several applications.
Dibas
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Department of Pharmacology, University of Noth Texas Health Science Center at Fort Worth, 76107, USA.
Yorio
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D000580:Amido Black; D000818:Animals; D001923:Brain Chemistry; D003101:Collodion; D004396:Coloring Agents; D004586:Electrophoresis / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D007202:Indicators and Reagents; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000032:analysis / Q000302:isolation & purification*; D051381:Rats; D012394:Rosaniline Dyes; D013194:Staining and Labeling
D004396:Coloring Agents; D007202:Indicators and Reagents; D009419:Nerve Tissue Proteins; D012394:Rosaniline Dyes; D003101:Collodion; C004692:coomassie Brilliant Blue; D000580:Amido Black