Fractionation of Water-Insoluble Protein Using Sephacryl S-200 in Formamide

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Abstract
The ability of Sephacryl S-200 to fractionate water-insoluble protein by gel permeation chromatography was investigated. Elution of protein standards from columns of Sephacryl S-200 equilibrated with formamide, an excellent solvent for both hydrophobic and hydro-philic proteins, was molecular weight dependent. Advantages of chromatography of water-insoluble proteins using Sephacryl S-200 include rapidity, recovery of protein free of detergent or solvent, safety, ability to purify large amounts of protein, and ability to separate proteins as large as 100, 000 daltons. Separation of water-insoluble polypeptides in a crude preparation of gliadin in formamide demonstrated the practicality of the method.