コンポジットレジンならびにアクリルレジンへのタンパク質の吸着
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概要
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It is well known that dental plaque plays an important role as a cause of inducing dental caries and periodontal diseases. The development of the dental plaque has been considered to be affected by the adsorption of some proteins in saliva and crevicular fluid on the surfaces of tooth and restoration. In this study, therefore, the adsorption behaviors of albumin, γ-globulin and lysozyme were investigated on composite resin, acrylic resin and hydroxyapatite. The adsorption isotherms showed that the adsorption of the proteins might be of the Langmuir type for the adsorbent subjects used. Albumin and γ-globulin tended to form an "end-on" monolayer with their globular molecules closely arranged on the surface of the adsorbents except for hydroxyapatite. Lysozyme, on the other hand, was adsorbed to form multiple layers with larger number of molecules. The amount of every adsorbed protein was considerable smaller for composite and acrylic resins than for hydroxyapatite. In any case, no significant changes in the adsorption were found by the pH changes within a range of 5.6-8.0 tested. It appeared on the hydroxyapatite that most of the adsorbed proteins were loosely bound and easily washed off. The formation of a tightly bound monolayer, however, was also recognized just on the surface of the hydroxyapatite as in the other subjects. The protein adsorption is generally larger on a hydrophobic surface than on a hydrophilic one. In this study, however, the adsorption was not increased on quartz surface even if its hydrophobicity was increased by silane treatment. It was also found that albumin was less adsorbed on composite resin having rough and complicated surface than on acrylic resin having smoother surface. These facts indicate that the protein adsorption may be influenced by some surface characteristics of the adsorbent other than its hydrophobicity and surface structure as well as by the interaction of the adsorbate with the adsorbent.
- 九州歯科学会の論文
- 1988-02-25
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