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Effects of phosphoric acid and glutaraldehyde‐HEMA on dentin collagen
Author(s) -
Ritter André V.,
Swift Edward J.,
Yamauchi Mitsuo
Publication year - 2001
Publication title -
european journal of oral sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.802
H-Index - 93
eISSN - 1600-0722
pISSN - 0909-8836
DOI - 10.1034/j.1600-0722.2001.00088.x
Subject(s) - dentin , hydroxylysine , phosphoric acid , glutaraldehyde , chemistry , hydroxyproline , distilled water , high performance liquid chromatography , chromatography , nuclear chemistry , hydrolysis , amino acid , lysine , biochemistry , dentistry , organic chemistry , medicine
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 1 or 5 min. An additional set of specimens was treated with 37% PA for 1 min followed by GD for 1 min. All specimens were washed with distilled water, lyophilized, reduced with standardized NaB 3 H 4 , 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.