Quantitation of proteins solubilized in sodium dodecyl sulfate-mercaptoethanol-tris electrophoresis buffer

✍ Scribed by Zahur Zaman; Robrecht L. Verwilghen

• Publisher: Elsevier Science
• Year: 1979
• Tongue: English
• Weight: 405 KB
• Volume: 100
• Category: Article
• ISSN: 0003-2697
• DOI: 10.1016/0003-2697(79)90110-6

✦ Synopsis

A simple method for determination of proteins, initially solubilized in Tris buffer containing sodium dodecyl sulfate (SDS), mercaptoethanol, and sucrose, is described. This method is based on protein and Coomassie brilliant blue G-250 binding but it involves the removal of excess SDS by precipitation with 100 mM potassium phosphate buffer, pH 7.4 to 7.5, prior to protein determination. It has been established that the precipitation of excess SDS does not lead to the removal of the solubilized proteins. Therefore the method is applicable to both water-soluble and water-insoluble protein samples.