The Macroheterogeneity of Type I Tyrosine-rich Proteins of Merino Wool

Abstract

The cystine-poor family of tyrosine-rich proteins of wool as their S-carboxymethyl derivatives has been shown by chromatography on quaternary ammonium ethylcellulose (QAE-cellulose) at pH 10· 5 to consist of 10 groups of proteins which span a threefold range of tyrosine content and vary in many other amino acids, particularly S-carboxymethylcysteine. Electrophoresis at pH 8·9 revealed that most fractions contain two or more components and by further chromatography of five of these groups at pH 8·3 on DEAE-cellulose 10 components have been isolated. The amino acid composition suggests that the components within each QAE-cellulose group are very closely related.