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Characterization of Low-molecular-weight Peptides in Human Parotid Saliva
H.E.R. Perinpanayagam
Departments of Dental Research and Biochemistry, University of Rochester, 601 Elmwood Avenue, Box 611, Rochester NY 14642
B.C. VanWuyckhuyse
Departments of Dental Research and Biochemistry, University of Rochester, 601 Elmwood Avenue, Box 611, Rochester NY 14642
Z.S. Ji
Department of Oral Sciences, School of Dentistry, University of Minnesota, 515 Delaware St. SE, Minneapolis, MN 55455
L.A. Tabak
The low-molecular-weight components of human saliva remain poorly characterized. Therefore, low-molecular-weight peptides (Mr < 3000) have been purified from human parotid saliva and characterized with respect to their amino acid sequence. From the sequences obtained, it is likely that these peptides are derived from proteolysis of the hydroxyapatite-interactive human salivary proteins, histatins, proline-rich proteins, and statherins. Since human parotid saliva is an amicrobial fluid, much of the low-molecular-weight peptide fraction of this secretion appears to be derived from the proteolytic processing of the larger proteins. Because of their small size, these peptides are likely to be in exchange with dental plaque fluid and may therefore help modulate events such as demineralization/remineralization, microbial attachment, and dental plaque metabolism at the tooth-saliva interface.
Key Words: parotid saliva • proteolytic cleavage • histatins • proline-rich proteins • statherin.
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Journal of Dental Research, Vol. 74, No. 1,
345-350 (1995)
DOI: 10.1177/00220345950740011001
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