Kinetics of the adsorption of salivary proteins to hydroxyapatite
Arancillo, Andrea A.
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The adsorption kinetics of proteins from human parotid and submandibular secretions were studied using hydroxyapatite. Protein was exposed to hydroxyapatite for a period ranging from 30 seconds to 12O minutes, and the adsorbed and unadsorbed fractions were subjected to slot blot analysis, polyacrylamide gel electrophoresis and amino acid analysis. A series of reconstituted secretions, each containing one of the salivary proteins in a biotinylated form was prepared to study the adsorption of each protein component in the presence of all the of the salivary proteins. After adsorption to hydroxyapatite for 30 sec to 120 minutes, the adsorbed fractions were analyzed by staining with alkaline phosphatase conjugated antibiotin antibodies. Salivary proteins as a whole adsorbed rapidly with an endpoint between 60 and 120 minutes. Individually, a faster adsorption process was observed for statherin and the smaller acidic proline-rich proteins. A more complex pattern, exhibiting a rapid phase followed by a slower phase, was characteristic of the larger acidic proline-rich proteins and histatins. These results suggest that there are different adsorption processes involved in the binding of salivary proteins to hydroxyapatite. These mechanisms include direct adsorption of protein to hydroxyapatite as well as indirect adsorption through interactions with hydroxyapatite-bound proteins.
PLEASE NOTE: This work is protected by copyright. Downloading is restricted to the BU community: please click Download and log in with a valid BU account to access. If you are the author of this work and would like to make it publicly available, please contact email@example.com.Thesis (M.Sc.D.)--Boston University, Henry M. Goldman School of Graduate Dentistry, 1994 (Periodontology and Oral Biology)Includes bibliographical references and index (leaves 81-93)
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