TY - JOUR
T1 - Characterization of in vivo salivary-derived enamel pellicle
AU - Al-Hashimi, I.
AU - Levine, M. J.
N1 - Funding Information:
Acknott~ledgemenrs-This work was supportedb y USPHS Grants DEO4518, DE04971. and Dental Research lnstitute Grant DE08240 from the National Institute of Dental Research. This study was based, in part, on a thesis submitted by I. Al-Hashimi to the Graduate School. State University of New York at Buffalo, for partial fulfilment of the requirements for the Doctor of Philosophy Degree. We wish IO acknowledge Dr Irwin Mandel (Center for Clinical Research in Dentistry. School of Dental and Oral Surgery. Columbia University) for his valuable discussions during the course of these studies.
PY - 1989
Y1 - 1989
N2 - 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 α-amylase, cysteine-containing phosphoprotein (CCP or cystatins), salivary mucin and sIgA. Glycosylated amylase was present in larger quantity than the non-glycosylated species. Only CCPI (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.
AB - 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 α-amylase, cysteine-containing phosphoprotein (CCP or cystatins), salivary mucin and sIgA. Glycosylated amylase was present in larger quantity than the non-glycosylated species. Only CCPI (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.
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U2 - 10.1016/0003-9969(89)90070-8
DO - 10.1016/0003-9969(89)90070-8
M3 - Article
C2 - 2480770
AN - SCOPUS:0024789499
SN - 0003-9969
VL - 34
SP - 289
EP - 295
JO - Archives of Oral Biology
JF - Archives of Oral Biology
IS - 4
ER -