Characterization of S-sulfokeratein from pig hair and its use as a modifier of type I collagen gel

Biosci Biotechnol Biochem. 2002 Jun;66(6):1382-5. doi: 10.1271/bbb.66.1382.

Abstract

S-sulfokeratein is prepared through S-sulfonation after the cleavage of disulfide bonds in keratin using ditiothreitol in urea. S-sulfokeratein is composed of two fractions, matrix and microfibril components, and S-sulfokeratein from the matrix component (Bs) can regenerate disulfide bonds. In this study, the effects of Bs and partially reduced Bs on type I collagen self-assembly and properties of reconstructed Bs- or partially reduced Bs-collagen gel were investigated. It was proved that collagen self-assembly was accelerated by the increased amount of added Bs, but partially reduced Bs with 10 mg DTT/100 mg Bs (Bs-10) did not affect the ratio of collagen self-assembly. The mechanical strength of Bs-collagen gel proved to be lower than control, but that of Bs-10-collagen gel was times higher than that of control.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biomechanical Phenomena
  • Collagen Type I / chemistry*
  • Gels / chemistry*
  • Hair / chemistry*
  • Keratins / analogs & derivatives*
  • Keratins / chemistry*
  • Protein Denaturation
  • Spectroscopy, Fourier Transform Infrared
  • Swine*

Substances

  • Collagen Type I
  • Gels
  • Keratins