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

Bioscience, Biotechnology and Biochemistry

Volumn 66, Issue 6, 2002, Pages 1382-1385

  Nomura, Yoshihiro ^a   Nakato, Hidetoshi ^a   Ishii, Yasuhiro ^a   Shirai, Kunio ^a  

^a TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

Author keywords

Collagen self assembly; Mechanical strength; Regeneration of disulfide bound; S sulfokeratein; Type I collagen

Indexed keywords

COLLAGEN TYPE 1; DRUG DERIVATIVE; KERATIN;

ANIMAL; ARTICLE; BIOMECHANICS; CHEMISTRY; GEL; HAIR; INFRARED SPECTROSCOPY; PROTEIN DENATURATION; SWINE;

ANIMALS; BIOMECHANICS; COLLAGEN TYPE I; GELS; HAIR; KERATINS; PROTEIN DENATURATION; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; SWINE;

SUS SCROFA;

EID: 0036615457     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.66.1382     Document Type: Article

References (18)

1. Powell, B. C. and Rogers, G. E., The role of keratin proteins and their genes in the growth, structure and properties of hair. In “Formation and Structure of Human Hair”, eds. Jolies, P., Zahn, H., and Hocker, H., Birkhauser Verlag, Base, pp. 59-148 (1997).
2. Richardson, R., Recent trends in the wool industry and some long-term policy issues. In “The Biology of Wool and Hair”, eds. Rogers, G. E., Reis, P. J., Ward, K. A., and Marshall, R. C., Chapman and Hall, London, pp. 1-14 (1989).
3. Kamal, A. M. S., Nomura, Y., Ishii, Y., and Shirai, K., Properties of bovine hair keratins solubilized with thioglycolate. JALCA, 93, 272-282 (1998).
4. Mies, H. H. and Zahn, H., Praparative gewinnung loslicher Proteine aus Wolle. Leder, 39, 1-9 (1988).
5. Mies, H. H. and Zahn, H., Gewinnung loslicher proteine aus wollabfall am beispiel des carbonisier-staubes. Leder, 39, 73-76 (1988).
6. Terashima, M., Yoshimura, K., Imai, T., Hozan, D., and Shirai, K.; Properties of protein extracted as s-sulfonate derivative from irradiated mink hair. Anim. Sci. J., 71, 76-82 (2000).
7. Takahashi, K., Nomura, Y., and Wada, K., Regulation of the collagen matrix reconstruction by repeating pepsin-digestion of insoluble collagen, Nippon Shokuhin Kogyo Gakkaishi, 36, 108-113 (1989).
8. Thomas H, In vitro reconstitution of wool intermediate filaments. Int. J. Biol. Macromol., 8, 258-264 (1986).
9. Erra, P., Gomez, N., Dolcet, L. M., and Julia, M. R., FTIR analysis to study chemical changes in wool following a sulfitolysis treatment. Textile Res. J., 67, 397-401 (1997).
10. Laemmli, U. K.; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
11. Nomura, Y., Takahashi, K., Shirai, K., and Wada, K., Features of collagen matrix reconstructed with proteodermatan sulfate from pigskin insoluble collagen. Agric. Biol. Chem., 53, 1614-1620 (1989).
12. Nomura, Y., Toki, S., Ishii, Y., and Shirai, K., Effect of transglutaminase on reconstruction and physicochemical properties of collagen gel from shark type I collagen. Biomacromolecules, 2, 105-110 (2001).
13. Douthwaite, F. J., Lewis, D. M., and Schumacher Hamedat, Reaction of cystine residues in wool with peroxy compounds. Textile Res. J., 63, 177-183 (1993).
14. Douthwaite, F. J., and Lewis, D. M., The formation of cysteine-s-sulphonate roups in wool and the effect on shrink-resistance. J. Soc. Dyers Colour., 110, 304-307 (1994).
15. Veis, A. and George, A., Fundamentals of interstitial collagen self-assembly; In “Extracellular Matrix Assembly and Structure”, eds. Yurchenco, P. D., Birk, D. E., Mecham, R. P., Academic Press, Ca., pp. 15-45 (1994).
16. Chandrasekhar, S., Kleinman, H. K., Hassell, J. R., Martin, G. R., Termine, J. D., and Trelstad, R. I., Regulation of type I collagen fibril assembly by link protein and proteoglycans. Collagen Rel. Res., 4, 323-338 (1984).
17. Nomura, Y., Takahashi, K., and Shirai, K., The role of proteodermatan sulfate from pigskin in in vitro collagen matrix reconstruction. Anim. Sci. Technol, 65, 33-41 (1994).
18. Snowden, J. M. and Swann, D. A., Effects of glycosaminoglycans and proteoglycan on the in vitro assembly and thermal stability of collagen fibrils. Biopolymers, 19, 767-780 (1980).