Degradation of Cu(II)-partly alkylated wool keratin complex by hygrogen peroxide.

Abstract

In order to obtain some information regarding the degradation or morphological components of wool keratin fiber brought about by hydrogen peroxide under conditions in which the Cu (II) ion is bound to wool keratin the degradation of partly alkylated wool keratin fiber prepared by alkylating the generated sulfhydyl groups with 2-vinylpyridine was studied for the Cu (II)-partly alkylated wool keratin complex/hydrogen peroxide system. At the early stage of the degradation, peptide fragments in the treat. ment solution were found to contain a large amount of s-β-(2-pyridylethyl) cysteine residue and the tyrosine content in the wool fiber residue, which belongs in quantity to high-glycine-tyrosine proteins of an amorphous matrix, increased as the initial degradation proceeded. These results suggest that the high-sulfur proteins were easily degraded in the peptide bond cleavage of these proteins, which are contained especially in the cuticle.