Electrophoretic analysis of salivary proteins from man and Macaca Fascicularis and immunological identification of salivary proline-rich proteins in the in-vivo, formed pellicle
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The purpose of this study was the electrophoretic analysis and comparison of salivary proteins from Man and Macaca fascicularis with particular emphasis on the presence of four anionic proteins, known as the major acidic praline-rich proteins (PRP I, PRP II, PRP III, PRP VI). The second part of this study constitutes an immunological approach to identify these salivary praline-rich proteins as constituents of the naturally formed, acquired enamel pellicle. The results obtained from disc gel and slab gel acrylamide electrophoresis indicated that the concentrations of praline-rich proteins (PRPs) present in human glandular secretions were higher than those measured for whole saliva. The latter, however, exhibited a heavily stained component known as serum albumin. Enzymes derived from oral microorganisms have been implicated in the degradation of PRPs in the oral environment leading to the electrophoretic changes observed. Des~ite the great similarities between parotid and submandibular saliva disc gel acrylamide electrophoretograms, at least one qualitative difference could be detected. [TRUNCATED]
Illustrations are black and white photographs.Thesis (M.Sc.D.)--Boston University, Henry M. Goldman School of Graduate Dentistry, 1979 (Oral Biology).
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