Characterization of S-sulfokeratein from pig hair and its use as a modifier of type I collagen gel.
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.
Nomura
Yoshihiro
Y
Faculty of Agriculture, Tokyo University of Agriculture and Technology, Fuchu, Japan. ny318@cc.tuat.ac.jp
Nakato
Hidetoshi
H
Ishii
Yasuhiro
Y
Shirai
Kunio
K
D000818:Animals; D001696:Biomechanical Phenomena; D024042:Collagen Type I / Q000737:chemistry*; D005782:Gels / Q000737:chemistry*; D006197:Hair / Q000737:chemistry*; D007633:Keratins / Q000031:analogs & derivatives* / Q000737:chemistry*; D011489:Protein Denaturation; D017550:Spectroscopy, Fourier Transform Infrared; D013552:Swine
D024042:Collagen Type I; D005782:Gels; D007633:Keratins