Abstract
Amino acid analyses of normal wools of several breeds and geographical origins are presented as evidence of the normal variation of composition. Some samples were from lots used for detailed comparative studies of fiber properties and processing behavior. A mohair sample was found to be similar to wool in composition. White Leghorn chicken feather keratin differed from wool in yielding larger amounts of serine and proline. Feather had characteristically smaller amounts of cystine and glutamic acid. Heterogeneity of wool and feather keratins was shown by differences in amino acid composition of fractions prepared by treatment with acid, by mechanical separation, or by partial solubilization in aqueous alcohol. Feather differs from wool in having readily separable fractions differing greatly in content of histidine, lysine, and methionine. These fractions also differ appreciably in their content of several other amino acids.
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