Abstract
High-sulfur proteins (γ-keratose) have been preferentially extracted from performic acid-oxidized wool with pyridine-acetate buffer (pH = 6.0). It has been shown that the γ-keratose is heterogeneous both on a charge and a molecular size basis by free electrophoresis, chromatography on DEAE-cellulose and calcium phosphate, and gel filtration on Sephadex. Four sub-fractions of γ-keratose which gave single peaks on electrophoresis and ultracentrifugation have been isolated by column electrophoresis. Thorough characterization has shown that these sub-fractions have very different physical properties and amino-acid compositions.
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