1995 Fiscal Year Final Research Report Summary
Kind and property of salivary proteins which adsorbed onto root surface
| Project/Area Number |
06672050
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
矯正・小児・社会系歯学
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| Research Institution | Okayama University |
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Principal Investigator |
KISHIMOTO Etsuo Okayama University Dental School, Department of Preventive Dentistry, Associate Professor. (1994,1995), 歯学部, 助教授 (20091316)
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| Project Period (FY) |
1994 – 1995
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| Keywords | Saliva / Protein / Dental pellicle / Dental caries / Root surface / Oral cavity / Electrophoresis / Microorganism |
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| Research Abstract |
Property of the tissue-surface affects on the adhesion of pathogenic bacteria to the host. There was the possibility that dental pellicle of the root surface differed from that of the enamel surface, because the root contains more amounts of organic components than enamel. The purpose of this study is to examine kinds and properties of salivary proteins, which adsorbed onto the root surface. Crown, root and artificial hydroxyapatite were immersed in submandibular-sublingual saliva or whole saliva allowed to adsorb salivary proteins. Protein adsorbed was recovered with sample buffer for sodium-dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) . SDS-PAGE running gels were stained with silver stain. Molecular-weights of proteins in submandibular-sublingual saliva were circa 300,180-145,86,60,59,55,43 kilodalton. Eluate contained only 180-145 kilodalton protein band. No significant difference of protein adsorbed was observed among three hard surfaces. Secondly, molecular-weights of proteins in whole saliva were circa 300-200,86,66,60,55 kilodalton. Whole saliva contained a significant amount of material, which did not penetrate into stacking gel. No band stained was detected. Probably adsorbable protein may be involved into aggregate and then did not remained in supernate of whole saliva. Gel-filtrated fraction containing of 180-145 kilodalton protein promoted the adhesion of S.sanguis onto the hard surface better than that of S.mutans. Isoelectrophoretic point of the protein was estimated circa five Adhesion promoting proteins (APP,Kishimoto et al., 1989) was mainly composed of serine, glycine, and glutamine and glutamic acid. These amino acids occupied approx. 40% of total protein.
Analysis of amino acid sequence suggests that N-terminal of APP might be blocked.
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