Loomis R E, Tseng C C, Levine M J
State University of New York, Buffalo, School of Dental Medicine.
Int J Pept Protein Res. 1988 Aug;32(2):123-9. doi: 10.1111/j.1399-3011.1988.tb00672.x.
The pKa's of the three histidine residues in a proline-rich glycoprotein from human parotid saliva (PRG) were determined by 360 MHz proton n.m.r. spectroscopy. The addition of calcium (0.64 mM) caused drops in the pKa's of all three histidines by approximately 0.25 units. When imidazole and cyclo)L-histidine-L-proline) were used as model compounds, corresponding concentrations of calcium had no effect on their pKa's. Also, the model compounds gave absolute pKa values in good agreement with similar chemical species reported in the literature. Exchange lifetime data and previously reported hydrogen----deuterium exchange experiments suggest that the PRG histidine N tau H protons are not involved in hydrogen-bonds. Collectively, these data imply that changes in PRG conformation occur upon the addition of calcium.
