Journal
EUROPEAN JOURNAL OF ORAL SCIENCES
Volume 109, Issue 5, Pages 348-353Publisher
WILEY
DOI: 10.1034/j.1600-0722.2001.00088.x
Keywords
collagen; cross-links; phosphoric acid; glutaraldehyde; dentin bonding
Categories
Funding
- NIDCR NIH HHS [DE10489] Funding Source: Medline
Ask authors/readers for more resources
The purpose of this study was to evaluate the effects of phosphoric acid (PA) and a proprietary glutaraldehyde-HEMA aqueous solution (Gluma Desensitizer. GD) on dentin collagen. Specimens of demineralized bovine dentin collagen were treated with either 37% or 50% PA for I or 5 min. An additional set of specimens was treated with 37% PA for I min followed by GD for I min. All specimens were washed with distilled water, lyophilized, reduced with standardized (NaBH4)-H-3, hydrolyzed with 6 M HCl and subjected to amino acid and cross-link analyses. The results demonstrated that the treatment of demineralized dentin with PA under the conditions tested did not significantly alter the collagen cross-links. The GD-treated samples showed reduction of free lysine (Lys) and hydroxylysine (Hyl) residues, as well as a decrease in the levels of collagen reducible cross-links. In addition, unidentified reducible compounds were detected by high-performance liquid chromatography (HPLC) analysis. These compounds may be derived from cross-links formed between GD-derived aldehyde and Lys/Hyl of collagen. The findings indicate that PA treatment does not significantly affect dentin collagen amino acid and cross-link composition, and that GD treatment affects dentin collagen amino acid and cross-link composition.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available