Characterization of in vivo salivary-derived enamel pellicle.
Journal - Archives of oral biology (ENGLAND )
Salivary proteins and glycoproteins that participate in the formation of 2-h in vivo enamel pellicle were determined utilizing polyacrylamide gel electrophoresis [sodium dodecyl sulphate (SDS)-PAGE and anionic PAGE]/Western transfer analyses, and specific radiolabelling/SDS-PAGE fluorography. The sensitivity of these methods permitted the identification of individual members of different salivary protein families. The major components of this pellicle were salivary alpha-amylase, cysteine-containing phosphoprotein (CCP or cystatins), salivary mucin and sIgA. Glycosylated amylase was present in larger quantity than the non-glycosylated species. Only CCP1 (cystatin SA-I) of the cysteine-containing phosphoprotein family was identified. The higher molecular-weight salivary mucin (MG1), but not the lower molecular-weight species (MG2), was detected. These results extend earlier observations regarding the selective nature of salivary protein adsorption to enamel surface by demonstrating that only specific members of salivary protein families are involved in 2-h in vivo enamel pellicle formation. The findings also suggest that individual family members may have different functions in the mouth.
|ISSN : ||0003-9969|
|Mesh Heading : ||Adult Amino Acids Amylases Cystatins Dental Deposits Dental Pellicle Electrophoresis, Polyacrylamide Gel Glycoproteins Humans Immunoglobulin A, Secretory Molecular Weight Mucins Saliva Salivary Cystatins Salivary Proteins and Peptides analysis analysis analysis analysis analysis physiology|
|Mesh Heading Relevant : ||analysis analysis analysis|