RESUMO
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.
