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The Influence of Molecular Structure on Apatite Adsorption

Published online by Cambridge University Press:  15 February 2011

S. A. Johnsson Mats
Affiliation:
Dept's of Biomaterials and Oral Biology, SUNY at Buffalo. Buffalo NY 14214.
P. A. Raj
Affiliation:
Dept's of Biomaterials and Oral Biology, SUNY at Buffalo. Buffalo NY 14214.
M. J. Levine
Affiliation:
Dept's of Biomaterials and Oral Biology, SUNY at Buffalo. Buffalo NY 14214.
G. H. Nancollas
Affiliation:
Dept's of Biomaterials and Oral Biology, SUNY at Buffalo. Buffalo NY 14214.
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Abstract

The hydroxyapatite (HAP) adsorption of salivary statherin, cystatins, proline-rich proteins and histatins has been compared to the influence of these molecules on HAP crystallization in supersaturated solution. This may yield, in many cases, information about protein conformation in the adsorbed state. The results of studies involving both parent molecules and their fragments, indicated that statherin binds to HAP primarily with a 2–5 residues segment in the N-terminal part while the cystatins and proline-rich proteins bind through a segment 2–3 times larger.

Type
Research Article
Copyright
Copyright © Materials Research Society 1992

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