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The Influence of Salivary Proteins on the Growth, Aggregation and Surface Properties of Hydroxyapatite Particles.

Published online by Cambridge University Press:  21 February 2011

M. Johnsson
Affiliation:
Dept's of Chem. and State University of New York at Buffalo, Buffalo, NY.
C. F. Richardson
Affiliation:
Dept's of Chem. and State University of New York at Buffalo, Buffalo, NY.
E. J. Bergey
Affiliation:
Oral Biol. State University of New York at Buffalo, Buffalo, NY.
F. A. Scannapieco
Affiliation:
Oral Biol. State University of New York at Buffalo, Buffalo, NY.
M. J. Levine
Affiliation:
Oral Biol. State University of New York at Buffalo, Buffalo, NY.
G. H. Nancollas
Affiliation:
Dept's of Chem. and State University of New York at Buffalo, Buffalo, NY.
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Abstract

The adsorption and crystal growth effects of salivary cystatin SA-II and non-glycosylated amylase on hydroxyapatite have been compared to the effects of the salivary cystatins SA-I and SA-III. Amylase was the least active HAP crystal growth inhibitor and adsorbed weakly to HAP. Although the three cystatins were active inhibitors of hydroxyapatite crystal growth in supersaturated solution, their affinities showed marked differences.

Type
Research Article
Copyright
Copyright © Materials Research Society 1990

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References

1. Hay, D.I. and Moreno, E.C., J. Dent. Res. 58B, 930 (1979).Google Scholar
2. Schlesinger, D.H. and Hay, D.I., J. Biol. Chem. 252, 1689 (1977).Google Scholar
3. Moreno, E.C. and Varughese, K., J. Cryst. Growth 53, 20 (1981).Google Scholar
4. Bennick, A., Chau, G., Goodlin, R., Abrams, S., Tustian, D. and Madapallimattam, G., Archs. oral Biol. 28, 19 (1983).Google Scholar
5. Al-Hashimi, I. and Levine, M.J., Archs. oral Biol. 34, 289 (1989).Google Scholar
6. Shomers, J.P., Tabak, L.A., Levine, M.J., Mandel, I.D. and Hay, D.I., J. Dent. Res. 61, 397 (1982)Google Scholar
7. van Kemenade, M.J.J.M. and De Bruyn, P.L., J. Coll. Interface Sci., 129, 1 (1989).Google Scholar
8. Johnsson, M., Richardson, C.F., Campbell, A.A., Bergey, E.J., Zawacki, S.J., Levine, M.J. and Nancollas, G.H., Archs oral Biol. Submitted for publication.Google Scholar
9. Wong, R.S.C., Hofmann, T. and Bennick, A., J. Biol. Chem. 254, 4800 (1979).Google Scholar
10. Wong, R.S.C. and Bennick, A., J. Biol. Chem. 255, 5943 (1980).Google Scholar
11. Schlesinger, D.H., Buku, A., Wyssbrod, H.R. and Hay, D.I., Int. J. Peptide Protein Res. 30, 257 (1987).Google Scholar
12. Bennick, A., Cannon, M. and Madapallimattam, G., Biochem. J. 183, 115 (1979).Google Scholar
13. Aoba, T., Moreno, E.C. and Hay, D.I., Calcif. Tissue Int. 36, 651 (1984).Google Scholar
14. Scannapieco, F.A., Bergey, E.J., Reddy, M.S. and Levine, M.J., Infect. Immun. 57, 2853 (1989).Google Scholar
15. Shomers, J.P., Tabak, L.A., Levine, M.J., Mandel, I.D. and Ellison, S.A., J.Dent. Res. 61, 973 (1982).Google Scholar
16. Al-Hashimi, I., Dickinson, D.P. and Levine, M.J., J. Biol. Chem. 263, 9381 (1988).Google Scholar
17. Hay, D.I., Bennick, A., Schlesinger, D.H., Minaguchi, K., Madapallimattam, G. and Schluckebier, S.K., Biochem. J. 255, 15 (1988).Google Scholar
18. Moreno, E.C., Kresak, M. and Hay, D.I., J. Biol. Chem. 257, 2981 (1982).Google Scholar
19. Bode, W., Engh, R., Musil, D., Thiele, U., Huber, R., Karshikov, A., Brzin, J., Kos, J. and Turk, V., The EMBO J. 7, 2593 (1988).Google Scholar
20. Hlady, V. and Furedi-Milhofer, H., J.Coll.Interf. Sci, 69, 460 (1979).Google Scholar