Influence of Viscosity and Thickener on the Effects of Bleaching Gels.

OBJECTIVE: This study investigated the influence of the viscosity and kind of thickener of 35% hydrogen peroxide bleaching gels on the tooth (color change, demineralization of enamel, and permeation) and on the gel [reactive oxygen species (ROS), pH, and peroxide concentration]. METHODS AND MATERIALS: Two hundred forty specimens were divided into groups of bleaching gels with different thickeners (CAR, carbomer; ASE, alkali swellable emulsion; MSA, modified sulfonic acid polymer; SSP, semisynthetic polysaccharide; PAC, particulate colloids) in three viscosities (low: 50,000 cP; medium: 250,000 cP; high: 1,000,000 cP). Color change (ΔEab), demineralization of enamel by Knoop microhardness (KHN) reduction analysis, and peroxide permeation (PP) were analyzed in the specimens, while pH, peroxide concentration (PC), and ROS were evaluated in the gels. Data were analyzed by two-way ANOVA (α=0.05). RESULTS: The higher viscosity gels reduced ΔEab, PP, enamel softening, and ROS in relation to the lower viscosity gels. However, the drop in pH and PC were higher in the more viscous gels. Gels with MSA produced higher ΔEab compared with SSP and ASE. The PP was higher for PAC, and smaller for SSP and CAR. The KHN reduction was higher for CAR and smaller for PAC. The higher pH reduction was seen for ASE and CAR, and the smaller for SSP. The PC reduction was higher for SSP and smaller for CAR. More ROS were observed for MSA and fewer for ASE. CONCLUSIONS: Increased gel viscosity was associated with reduced color change, permeation, demineralization of enamel, and ROS, and led to increased peroxide decomposition and pH alteration during the treatment. The kind of thickener significantly interfered with the treatment effects.

Multiple unfolded states of glutathione transferase bbGSTP1-1 by guanidinium chloride.

Inactivation, dissociation, and unfolding of the homodimeric glutathione transferase (bbGSTP1-1) from Bufo bufo embryos were investigated at equilibrium, using guanidinium chloride (GdmCl) as denaturant. Protein transitions were monitored by enzyme activity, intrinsic fluorescence, far UV circular dichroism, glutaraldehyde cross-linking, and gel-filtration chromatography. At low denaturant concentrations (less than 0.5 M), reversible inactivation of the enzyme occurs. At denaturant concentrations between 0.5 and 1.5 M the enzyme progressively dissociates into structured monomers. At higher denaturant concentrations the monomers unfold completely. Refolding studies indicate that a total reactivation occurs only by starting from the enzyme denatured at concentrations below 0.5 M. The enzyme denatured at GdmCl concentrations higher than 0.5 M only partially refolds. Globally our results indicate that unfolding of the amphibian bbGSTP1-1 is a multistep process, i.e., inactivation of the structured dimer, dissociation into partially structured monomers, followed by complete unfolding.

Characterization of toad liver glutathione transferase.

The major form of glutathione transferase from the toad liver previously designed as Bufo bufo liver GST-7.6 (A. Aceto, B. Dragani, T. Bucciarelli, P. Sacchetta, F. Martini, S. Angelucci, F. Amicarelli, M. Miranda and C. Di Ilio, Biochem. J. 289 (1993) 417-422) has been characterized. According to its partial amino acid sequence, the toad enzyme may be included in the pi class GST and named bbGST P2-2. However, bbGST P2-2 appears to be immunologically, structurally and kinetically distinct from any other members of pi family, including bbGST P1-1, suggesting that it may constitute a subset of pi class GST. The data support the hypothesis that the transition from aquatic to terrestrial life causes a switch of the GST amphibian pattern promoting the expression of a GST form (bbGST P2-2) able to counteract, with higher efficiency, the toxic effects of reactive metabolites of oxidative metabolism and those of hydrophobic xenobiotics.