The Possibility of Common Amino Acid Sequences in High-Sulphur Protein Fractions from Wool

Abstract

S-Carboxymethyl derivatives of the high-sulphur components of reduced Merino wool have been subdivided by chromatography into 17 fractions, the amino acid compositions of which are reported. Tryptic, chymotryptic, and thermolysin digests of each fraction have been studied by high-voltage paper electrophoresis at pH 3·5 and 6·5. The results suggest that the high-sulphur proteins consist of families of proteins probably containing common structural features. Evidence is presented that the heterogeneity of high-sulphur proteins is not artefactual.