Biochemical Characterization of Recombinant Mouse Amelogenins: Protein Quantitation, Proton Absorption, and Relative Affinity for Enamel Crystals

References

• Hu C.-C., Ryu O. H., Qian Q., Zhang C. H., Simmer J. P. Cloning, characterization and heterologous expression of murine exon 4-containing amelogenin mRNAs. J. Dent. Res. 1997; 76: 641–647
   PubMed Web of Science ®Google Scholar
• Simmer J. P., Hu C. C., Lau E. C., Sarte P., Slavkin H. C., Fincham A. G. Alternative splicing of the mouse amelogenin primary RNA transcript. Calcif. Tissue Int. 1994; 55: 302–310
   PubMed Web of Science ®Google Scholar
• Ryu O. H., Hu C.-C., Simmer J. P. Comparative HPLC, SDS-PAGE, and immunoblot analyses of dental enamel proteins. Adv. Dent. Res. 1996; 10: 150–158
   PubMedGoogle Scholar
• Simmer J. P., Fincham A. G. Molecular mechanisms of dental enamel formation. [Review]. Crit. Rev. Oral Biol. Med. 1995; 6: 84–108
   PubMedGoogle Scholar
• Simmer J. P., Snead M. L. Molecular biology of the amelogenin gene. Dental Enamel: Formation to Destruction, C. Robinson, J. Kirkham, R. Shore. CRC Press, Boca Raton 1995; 59–84
   Google Scholar
• Dental Enamel Formation to Destruction, C. Robinson, J. Kirkham, R. Shore. CRC Press, Boca Raton 1995; 1–243
   Google Scholar
• Fukae M., Tanabe T., Shimizu M. Proteolytic enzyme activity in porcine immature enamel. Tsurumi U. Dent. J. 1977; 3: 15–17
   PubMedGoogle Scholar
• Yamakoshi Y., Tanabe T., Fukae M., Shimizu M. Porcine amelogenins. Calcif. Tissue Int. 1993; 54: 69–75
   Web of Science ®Google Scholar
• Fincham A. G., Moradian-Oldak J. Recent advances in amelogenin biochemistry. [Review]. Conn. Tis. Res. 1995; 32: 119–124
   PubMed Web of Science ®Google Scholar
• Brookes S. J., Robinson C., Kirkham J., Bonass W. A. Biochemistry and molecular biology of amelogenin proteins of developing dental enamel. [Review]. Arch. Oral Biol. 1995; 40: 1–14
   PubMed Web of Science ®Google Scholar
• Fincham A. G., Moradian-Oldak J. Comparative mass spectrometric analyses of enamel matrix proteins from five species suggest a common pathway of post-secretory proteolytic processing. Conn. Tis. Res. 1996; 35: 151–156
   PubMed Web of Science ®Google Scholar
• Uchida T., Tanabe T., Fukae M., Shimizu M., Yamada M., Miake K., Kobayashi S. Immunochemical and immunohistochemical studies, using antisera against porcine 25 kDa amelogenin, 89 kDa enamelin and the 13–17 kDa non-amelogenins, on immature enamel of the pig and rat. Histochemistry 1991; 96: 129–138
   PubMedGoogle Scholar
• Fincham A. G., Lau E. C., Simmer J. P., Zeichner-David M. Amelogenin Biochemistry-Form and Function. Chemistry and Biology of Mineralized Tissues, H. C. Slavkin, P. Price. Elsevier Scientific Publishers, Amsterdam 1992; 187–202
   Google Scholar
• Simmer J. P., Lau E. C., Hu C. C., Aoba T., Lacey M., Nelson D., Zeichner-David M., Snead M. L., Slavkin H. C., Fincham A. G. Isolation and characterization of a mouse amelogenin expressed in Escherichia coli. Calcif. Tissue Int. 1994; 54: 312–319
   PubMed Web of Science ®Google Scholar
• Moradian-Oldak J., Simmer J. P., Lau E. C., Sarte P. E., Slavkin H. C., Fincham A. G. Detection of monodisperse aggregates of a recombinant amelogenin by dynamic light scattering. Biopolymers 1994; 34: 1339–1347
   PubMed Web of Science ®Google Scholar
• Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 1951; 193: 265–275
   PubMed Web of Science ®Google Scholar
• Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-bye binding. Anal. Chem. 1976; 72: 248–254
   Google Scholar
• Aoba T., Moreno E. C. The enamel fluid in the early secretory stage of porcine amelogenesis: chemical composition and saturation with respect to enamel mineral. Calcif Tissue Int 1987; 41: 86–94
   PubMed Web of Science ®Google Scholar
• Creighton T. E. Proteins: Structures and Molecular Properties. W. H. Freeman and Company, New York 1993; 507
   Google Scholar
• Samachson J. Mechanism of exchange of inorganic phsophate with bone mineral and its relation to the mechanism of calcification. Nature 1968; 218: 1262–1263
   PubMed Web of Science ®Google Scholar
• Samachson J. Basic requirements for calcification. Nature 1969; 221: 1247–1248
   PubMed Web of Science ®Google Scholar
• Aoba T., Fukae M., Tanabe T., Shimizu M., Moreno E. C. Selective adsorption of porcine-amelogenins onto hydroxyapatite and their inhibitory activity on hydroxy-apatite growth in supersaturated solutions. Calcif Tissue Int. 1987; 41: 281–289
   PubMed Web of Science ®Google Scholar
• Addadi L., Weiner S. Stereochemical and structural relations between macromolecules and crystals in biomineralization. Biomineralization, Chemical and Biochemical Perspectives, S. Mann, J. Webb, R. J.P. Williams. Weinheim, New York 1989; 133–152
   Google Scholar