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dc.contributor.authorDamiani, Francescoen_US
dc.date.accessioned2020-11-05T16:14:20Z
dc.date.available2020-11-05T16:14:20Z
dc.date.issued1995
dc.date.submitted1995
dc.identifier.other(OCoLC)38426800
dc.identifier.otherb21845050
dc.identifier.urihttps://hdl.handle.net/2144/41597
dc.descriptionPLEASE 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 open-help@bu.edu.en_US
dc.descriptionThesis (M.Sc.D.)--Boston University. Henry M. Goldman School of Graduate Dentistry, 1995 (Periodontology and Oral Biology).en_US
dc.descriptionIncludes bibliographic references (leaves 62-75).en_US
dc.description.abstractThe acquired enamel pellicle, the in vivo pellicle, is a thin protein layer that arises from the adsorption of salivary proteins onto the enamel surface of teeth. One of its roles is to maintain the integrity of the tooth surface by affecting both demineralization and remineralization processes. In addition, the acquired enamel pellicle is the substrate on which initial bacterial colonization takes place, a process which depends upon the nature of the pellicle. ln this study, the two hour in vivo formed enamel pellicle was characterized and compared to the two hour in vitro formed pellicle derived from pure parotid secretion. Amino acid analysis, high sensitivity SDS p01yacrylamide gel electrophoresis, both anionic and cationic polyacrylamide gel electrophoresis and Western blot analysis were used to study the composition of in vivo pellicle. The antibodies for Western blot analysis were selected based upon in vitro studies demonstrating the affinity of certain salivary proteins to hydroxyapatite. Since the amino acid composition of acquired enamel pellicle is different from those of parotid and submandibular secretions, the pe11icle is composed of selectively adsorbed proteins. Based on the electrophoretic results from Tricine buffered, highly crosslinked, polyacrylamide gels, the acquired enamel pel1icle contains approximately 25 proteins or peptides ranging in apparent molecular weightS from 200 kDa to 7 kDa. This is surprising since in vitro models using salivary secretions contain approximately five components on these gels. It is also interesting to note that of the proteins tested by Western blot analysis, only one, amylase, was clearly detected. Proline-rich proteins, statherin, and histatins readily identified in in vitro pellicles were below the levels of detection in the in vivo formed pel1icle. These results suggest that the in vivo enamel pellicle is composed of some proteins from salivary secretions in their intact form and other proteins which may be proteolytically degraded salivary proteins, complexes of salivary proteins, or proteins of nonsalivary origin.en_US
dc.language.isoen_US
dc.publisherBoston Universityen_US
dc.rightsThis work is protected by copyright. Downloading is restricted to the BU community. If you are the author of this work and would like to make it publicly available, please contact open-help@bu.edu.en_US
dc.subjectDental enamel proteinsen_US
dc.titleElectrophoretic and immunological characterization of the acquired enamel pellicleen_US
dc.typeThesis/Dissertationen_US
etd.degree.nameMaster of Science in Dentistryen_US
etd.degree.levelmastersen_US
etd.degree.disciplinePeriodontology and Oral Biologyen_US
etd.degree.grantorBoston Universityen_US


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