AbstractSilk fibroin is crosslinked by 0.1–1.0Mammonium peroxydisulfate at 70°C. or at 40°C. in the presence of silver ion. Induced decomposition of peroxydisulfate in the presence of fibroin is observed. Methylation of tyrosine in fibroin does not slow attack by peroxydisulfate, but crosslinking of the fibroin is prevented. Modification of tryptophan with α‐bromo‐5‐nitro‐2‐cresol does not prevent crosslinking by peroxydisulfate, however. The nature and sites of crosslinking in fibroin are suggested in light of physical and chemical data, amino acid analyses of crosslinked and control fibroins, and the known mode of decomposition of p
展开▼
