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Salivary proteins include numerous functional proteins which play important roles not only for the food-intake but also for the
protective and defensive mechanisms. In the present study the compositions of salivary proteins were analyzed by different methods,
including electrophoresis and high performance liquid chromatography (HPLC). In hydrophobic protein HPLC analysis the parotid saliva
gradually produced macromolecular complexes when agitated in refrigerator until 30 minutes. These salivary protein complexes were
digested by neuraminidase, and then migrated more rapidly in native tris glycine gel than the control. Therefore, it was assumed that
the glycosylated proteins of parotid saliva became gradually aggregated to form salivary protein complexes similar to those of whole
saliva. The salivary protein complexes were easily degenerated in different experimental buffers, i.e., SDS buffer, tris glycine buffer,
methanol, etc., and resulted non-specific patterns in electrophoresis and HPLC. Therefore, it was presumed that the salivary protein
complexes was made by the hydrophobic interaction as well as electrostatic attraction between salivary proteins. These data indicated
that to know the real pattern of salivary protein complexes in vivo the whole saliva should be analyzed by HPLC using non-adhering
column with isoelectric buffer. Consequently, the whole saliva was analyzed by HPLC using reverse phase SuperoseTM column with
20 mM potassium phosphate buffer, and two prominent peaks of salivary protein complexes were consistently found in every people.
These salivary protein complex peaks were relatively stable up to 6 hours after saliva collection when the whole saliva was kept
in refrigerator during experiment. Therefore, it is suggested that the salivary protein complex patterns are characteristic macromolecular
structures of whole saliva, which are also applicable as a diagnostic point in different saliva-associated diseases.