STUDY ON REFOLDING OF ACTIVE KERATINS

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keratins, which are proteins bearing cysteine as much as 10 mole % of total amino acid residues, were extracted from wool and hair as a stable aqueous solution. Chief constituents of the proteins had molecular weight ranging from 40000 to 60000 and an isoelectric point of about 6. The aqueous keratin solution was casted into the clear thin film readily. The film showed high tensile strength and underwent biodegradation by trypsin and other proteases as well as under mouse skin. Both in vitro and in vivo degradations were much slower than the protein film prepared from collagen.TEM and SEM revealed that the keratins in the film were fabricated to a thin thread although a quantitative preparation method has not been established yet. The refolding of the active keratins has been investigated using a purified keratin molecule rather.