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Objective: To observe the effect of purified high rela ti ve molecular mass mucin(MG1) pellicle on the protection of human dental enamel against demineralization.Methods: MGI was extracted from human saliva and purified.MGI pellicle and whole saliva pellicle were formed on dental enamel samples in vitro ,Then The samples were treated by 34 mmol/L citric acid for 1 min.The demineralization of the samples was observed by scanning electronic microscopy(SEM). Results:After treatment by the acid the enamel surfaces covered by MGI pellicles or whol e saliva pellicle showed relatively smooth and normal enamel morphological feat ures, on the contrary the surface without pellicle showed large area of deminer alization and bee nest like appearance. Conclusion: The data indicate that the MG1 in enamel pellicle contribute to its protective effec ts against acidic attack on the enamel surface.
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0bjective: To observe the effects of parotid saliva(PARS), extraparotid saliva(EPS) and purified high molecular weight mucin(MG1) on the aggregation of streptococcus mutans . Methods: PARS, EPS and MG1 were prepared routinely and applied in the cultures of S. mutans Inbritt, S.mutans LM and S.sobrinus OMZ 176 respectively for 2 h. The aggregation of the bacteria was measured spectrophotometrically.Results: The aggregation (%) of S.mutans Inbritt, S.mutans LM and S.sobronus OMZ 176 induced by EPS was 32.80 , 57.87 and 35.46 , that by MGI 25.68, 32.77 and 24.16 , that by PARS 13.52, 22.23 and 16.00, respectively. Conclusion: The effect of MGI on the aggregation of streptoccus mutans is weaker than that of EPS and stronger than that of PARS. The aggregation may be primarily induced by mucins.
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0.01). Conclusion: Occlusal reduction might diminish the rate of postoperative pain following endodontic instrumentation.
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砄bjective:To purify and characterize human high molecular eight salivary mucin(MG1).Methods: MG1 was purified by 10%(w/v) cetyltrimethylammonium bromid precipitation, CM Sephadex ion exchange chromatography and sephadax G 200 gel filtration chromatography. The protein content was studied with Folinin Lowrys analysis and characterized by PAGE and SDS PAGE electrophoresis.Results:The data of PAGE showed that the purified glycoprotein was free of contaminating proteins;those SDS PAGE showed that the melocular weight of the glycoprotein was between Mr 500 000 and 1 000 000.Protein quantitative analysis showed that it contained 14.17% of protein.Amino acid analysis revealed that it contained 17 kinds of amino acid;Thr,Ser,Pro and ALa were the dominant amino acid(45.6% of the total).Conclusion: The data indicate the applied technique is reliable for purification MG1 from saliva.