SummaryThe low-sulphur wool protein SCMKA2, which gives only single peaks on electrophoresis and ultracentrifugation over a wide range of pH and concentration, has been divided arbitrarily by ammonium sulphate precipitation into two fractions. Amino acid analysis has shown significant differences between the fractions in some amino acid residues, particularly of S-carboxymethyl cysteine, glycine, phenylalanine, tyrosine, and valine. Both fractions have been shown to be heterogeneous by chromatography on DEAE-cellulose and elution with buffer containing 8M urea. One fraction, that which is less soluble in ammonium sulphate, has the lowest sulphur content of any wool protein so far separated. From this fraction a subfraction was prepared by column chromatography which differed significantly in amino acid composition from either of the ammonium sulphate fractions. These data are consistent with the hypothesis that there are a number of low-sulphur proteins in wool.