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Bioscience, Biotechnology, and Biochemistry Volume 70, 2006 - Issue 4
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Original Articles

Improved Physical and Biochemical Features of a Collagen Membrane by Conjugating with Soluble Egg Shell Membrane Protein

Tamao INODepartment of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology
,
Makoto HATTORIDepartment of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology
,
Tadashi YOSHIDADepartment of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology
,
Shunji HATTORINippi Research Institute of Biomatrix, Senju-Midoricho, Nippi Inc.
,
Keiji YOSHIMURATokyo Metropolitan Leather Technology Center
&
Koji TAKAHASHIDepartment of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology
Pages 865-873 | Received 07 Sep 2005, Accepted 01 Dec 2005, Published online: 22 May 2014

  • 1) Tann, C. K., Chen, T. W., Chen, H. L., and Ng, L. S., A scanning and transmission electron microscopic study of the membrane of chicken egg. Histol. Histophath., 7, 339–345 (1992).
  • 2) Baker, J. R., and Balch, D. A., A study of organic material in hen’s-egg shell. Biochem. J., 82, 352–361 (1962).
  • 3) Suyama, K., Nakamura, H., Ishida, M., and Adachi, S., Lipids in the exterior structures of the hen egg. J. Agric. Food Chem., 25, 799–803 (1977).
  • 4) Maeda, K., and Sasaki, Y., An experience of hen-egg membrane as a biological dressing. Burns, 8, 313–316 (1981).
  • 5) Suyama, K., and Fukazawa, Y., A new biomaterial, hen egg shell membrane, to eliminate heavy metal ion from their dilute waste solution. Appl. Biochem. Biotech., 45, 871–879 (1994).
  • 6) Ishikawa, S., Suyama, K., Arihara, K., and Itoh, M., Uptake and recovery of gold ions from electrolpolating wastes using eggshell membrane. Bioresour. Technol., 81, 201–206 (2002).
  • 7) Ishikawa, S., Suyama, K., and Itoh, M., Biosorption of acinides from dilute waste actinide solution by egg-shell membrane. Appl. Biochem. Biotechnol., 77–79, 521–533 (1999).
  • 8) Crombie, G., Snider, R., Faris, B., and Franzblau, C., Lysine-derived cross-links in the egg shell membrane. Biochim. Biophys. Acta, 640, 365–367 (1981).
  • 9) Leach, R. M., Rucker, R. B., and Duke, G. P., Egg shell membrane protein; a nonelastin desmosine/isodesmosine-containing protein. Arch. Biochem. Biophys., 207, 353–359 (1981).
  • 10) Takahashi, K., Shirai, K., Kitamura, M., and Hattori, M., Soluble egg shell membrane protein as a regulating material for collagen matrix reconstruction. Biosci. Biotechnol. Biochem., 60, 1299–1302 (1996).
  • 11) Takahashi, K., Shirai, K., and Hattori, M., Conjugated film from reconstruction of collagen-soluble egg shell membrane protein matrix. Anim. Sci. Technol., 67, 862–868 (1996).
  • 12) Ehrlich, H. P., Understanding experimental biology of skin equivalent: from laboratory to clinical use in patients with burns and chronic wounds. Am. J. Surg., 187, 29S–33S (2004).
  • 13) Ruszczak, Z., Effect of collagen matrices on dermal wound healing. Adv. Drug Deliv. Rev., 55, 1595–1611 (2003).
  • 14) Bello, Y. M., Falabella, A. F., and Eaglstein, W. H., Tissue-engineered skin. Current status in wound healing. Am. J. Clin. Dermatol., 2, 305–313 (2001).
  • 15) Masahiro, K. O., and Taya, M., Development of culture techniques of keratinocytes for skin graft production. Adv. Biochem. Eng. Biotechnol., 91, 135–169 (2004).
  • 16) Robert, M., Dusser, I., Muriel, M. P., Noel-Hudson, M. S., Aubery, M., and Welpierre, J., Barrier function of reconstructed epidermis at the air-liquid interface: influence of dermal cells and extracelluar components. Skin Pharmacol., 10, 247–260 (1997).
  • 17) Takahashi, K., and Hattori, M., Edible meat casing from reconstruction of collagen-elastin matrix. J. Food Sci., 58, 734–738 (1993).
  • 18) Takahashi, K., Shirai, K., and Wada, K., Melting behavior of gels prepared from isolated subunits of collagen. J. Food Sci., 53, 1920–1921 (1988).
  • 19) Takahashi, K., Ogata, A., Yang, W.-H., and Hattori, M., Increased hydrophobicity of carboxymethyl starch film by conjugating with zein. Biosci. Biotechnol. Biochem., 66, 1276–1280 (2002).
  • 20) Hattori, S., Adachi, E., Ebihara, T., Shirai, T., Someki, I., and Irie, S., Alkali-treated collagen retained the triple helical conformation and the ligand activity for the cell adhesion via alpha2beta1 integrin. J. Biochem., 125, 676–684 (1999).
  • 21) Dubois, M., Gilles, K. A., Hamilton, J. K., Reber, P. A., and Smith, F., Colorimetric method for determination of sugars and related substances. Anal. Chem., 28, 350–356 (1956).
  • 22) Bitter, T., and Muuir, H. M., A modified uronic acid carbazole reaction. Anal. Biochem., 4, 330–334 (1962).
  • 23) Gardell, S., Separation of Dowex 50 ion-exchange resin of glucosamine and galactosamine, and their quantitative determination. Acta Chem. Scand., 7, 207–215 (1953).
  • 24) Hattori, M., and Takahashi, K., Pepsin-solubilized elastin as a water/oil emulsifier. Food Hydrocolloids, 7, 327–335 (1993).
  • 25) Nakazaki, S., Takaku, K., Yuguchi, M., Edamatsu, H., and Takahashi, K., Regulation of molecular structure of acid-dispersed collagen with alkaline pretreatment. Anim. Sci. Technol., 65, 1018–1025 (1994).
  • 26) Kim, J. P., Chen, J. D., Wilke, M. S., Schall, T. J., and Woodley, D. T., Human keratinocyte migration on type 4 collagen. Role of heparin-binding site and alpha2beta1 integrin. Lab. Invest., 71, 401–408 (1994).
  • 27) Burridge, K., Gath, K., Kelly, T., Nuckolls, G., and Turner, K., Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Ann. Rev. Cell Biol., 4, 487–525 (1988).

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