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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https://hdl.handle.net/2144/35612Abstract
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]
Description
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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