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Abstract
Various methods of splitting disulphide bonds have been applied to wool Extractions of the disulphide-free wools have given protein fractions of higher and lower sulphur contents than normal wool. Amino-acid analyses of various fractions are given. The low-sulphur proteins have been shown to aggregate extensively in solution. The light-scattering method has been used to study their disaggregation by various reagents both in aqueous and non-aqueous solvents. No obvious relation exists between the configuration, as measured by optical rotation, and the state of aggregation in a particular solvent. Digestion by trypsin of a low-sulphur fraction and subsequent chromatography of the peptides has not revealed a simple pattern which would be expected from a homogeneous protein.
