The Isolation and Properties of Some Soluble Proteins from Wool IV. The Isolation of the High-Sulphur Protein Scmkb1

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Abstract
A protein of high sulphur content (6.7% S) has been separated from the S-carboxymethyl derivatives of the high-sulphur proteins of Merino wool by salting-out and chromatography on DEAE-cellulose. Amino acid analysis shows that this modified protein is extremely rich in S-carboxymethyl cysteine, almost one residue in every four being accounted for by this residue, and it is also rich in serine, threonine, and proline; these four residues together account for almost two-thirds of the weight of the protein. It contains no methionine and only small amounts of lysine, histidine, phenylalanine, and aspartic acid. About 0.6% sulphur, based on the dry weight of the protein, is unaccounted for. This protein appears to have a molecular weight of between 25,000 and 28,000.