Characterisation Studies on the Specific Human Salivary Proteins Adsorbed in vitro by Hydroxyapatite

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Abstract
Disc electrophoresis studies of the in vitro adsorption on hydroxyapatite (HA) of human salivary supernatant proteins confirmed a preferential uptake of 4 electrophoretically homogeneous proteins, 3 of which derived predominantly from the parotid secretion. Amino acid analysis of the adsorbed complex also inferred a parotid secretion origin, indicated by its high proline content. Following column iso-electric focusing of the salivary proteins, fractions were examined for their amino acid composition. One electrophoretically homogeneous protein was characterised by a high proline content and high pi (c. 9) and shown to be adsorbed by HA. Another salivary protein component (pi, c. 7) was similarly adsorbed by HA. Both proteins were shown by disc electrophoresis to be co-incident in position with 2 of the 3 parotid secretion proteins specifically adsorbed by HA. It is postulated that these parotid proteins might contribute to the in vivo formation of the first formed integumental structures acquired post-eruptively by the tooth enamel surfaces.

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