Chicken feather keratin was solubilized by reduction with 2-mercaptoethanol under various conditions with different pH and the effect of solubilization conditions on the physical and chemical properties of solubilized proteins were examined.The extent of solubilization of feather keratin was different with pH of solvents used for its reduction. SDS-polyacrylamide gel electrophoresis of the solubilized keratin derivative showed the presence of four to five components and suggested that the components were heterogeneous with respects of net charges and/or molecular weights.Molecular sieve chromatography with Sephadex G-200 column and ultracentrifugation measurements as well as SDS-polyacrylamide gel electrophoresis showed that the proteins solubilized consisted of a major component with a molecular weight of approximately 10,000 and its various aggregates.
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