The Fractionation of the High-Sulfur Proteins from Oxidized Mohair

Abstract

The high-sulfur proteins (γ-keratose) of performic acid-oxidized mohair have been fractionated by a combination of column electrophoresis and gel filtration. The sub fractions revealed single peaks when examined by free electrophoresis and gel filtration at pH 4 and chromatography on DEAE-cellulose at pH 4.5. Data are presented con cerning the electrophoretic mobilities, molecular weights and amino acid compositions of the subfractions. End-group determinations revealed various N-terminal amino acids for some of the subfractions and confirmed the microheterogeneous nature of these fractions. In addition, some of the proteins of mohair γ-keratose were presumably present as aggregates in aqueous solution.