Characterization of in vivo salivary-derived enamel pellicle.

Abstract:

: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.

journal_name

Arch Oral Biol

journal_title

Archives of oral biology

authors

Al-Hashimi I,Levine MJ

doi

10.1016/0003-9969(89)90070-8

subject

Has Abstract

pub_date

1989-01-01 00:00:00

pages

289-95

issue

4

eissn

0003-9969

issn

1879-1506

pii

0003-9969(89)90070-8

journal_volume

34

pub_type

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