Structural Probe Analysis on the Attachment of Salivary Glycoproteins to Hydroxyapatite Using Fourier-Transformed Infrared Spectroscopy
| Autor: | D.R.J. Green, G. Embery, G. Rölla |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
Chemical Phenomena
Spectrophotometry Infrared Dental pellicle Infrared spectroscopy Apatite Absorption chemistry.chemical_compound Spectrophotometry Amide medicine Humans Moiety Dental Pellicle Salivary Proteins and Peptides General Dentistry Glycoproteins chemistry.chemical_classification Chromatography Fourier Analysis medicine.diagnostic_test Chemistry Physical Chemistry Carbohydrate Crystallography Clusterin visual_art visual_art.visual_art_medium Hydroxyapatites Glycoprotein Molecular Chaperones |
| Zdroj: | Caries Research. 23:247-251 |
| ISSN: | 1421-976X 0008-6568 |
| DOI: | 10.1159/000261186 |
| Popis: | The mechanisms of interaction between a salivary glycoprotein and hydroxyapatite has been studied using Fourier-transformed infrared spectroscopy. The spectra of the reacted mixtures showed evidence of change at 1,230-1,250 cm-1 due to the S = O stretching vibrations of the ester sulphate groups and at 775 and 828 cm-1 attributed to sulphate groups in the 6-position of N-acetylgalactosamine. Evidence of amide change in the regions of 1,670 and 1,550 cm-1 is also apparent due to involvement of the polypeptide region. It is proposed that the exposed parts of the protein core are involved in the attachment of the glycoprotein to hydroxyapatite with the main interactive residues being the sulphate groups present on the carbohydrate apo-protein moiety. The results are considered of value in relation to mechanisms involved in the coating of exposed apatite surfaces during the formation of acquired enamel pellicle. |
| Databáze: | OpenAIRE |
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