Abstract
1. A solution of silk fibroin (Bombyx mori) in 6 M urea was prepared using conditions under which peptide bonds are stable. 2. By disc electrophoresis the fibroin solution was separated into three strong and several weak zones. 3. Short-time extraction of fibroin fibres with a solution of lithiumthiocyanate yielded a soluble fraction (4% by weight) with an amino acid composition, different from fibroin. 4. On DEAE-cellulose columns the fibroin solution in 6 M urea was separated into two fractions. The amino acid composition of one of these fractions differed markedly from that of fibroin.
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