Effect of initiator and inhibitor concentration on the polymerization shrinkage kinetics of experimental dental composites

2014 ◽  
Vol 41 (1) ◽  
Author(s):  
Eun-Jung Sang
2014 ◽  
Vol 30 ◽  
pp. e57
Author(s):  
H. Al-Sunbul ◽  
N. Silikas ◽  
D.C. Watts

2014 ◽  
Vol 39 (4) ◽  
pp. 374-382 ◽  
Author(s):  
HM El-Damanhoury ◽  
JA Platt

SUMMARY The present study assessed the polymerization shrinkage stress kinetics of five low-shrinkage light-cured bulk-fill resin composites: Surefil SDR flow (SF, Dentsply), Tetric EvoCeram Bulkfil (TE, Ivoclar Vivadent), Venus Bulk Fill (VB, Heraeus Kulzer), x-tra fil (XF, Voco), and experimental bulk fill (FB, 3M ESPE). Filtek Z250 (FZ, 3M ESPE) was used as a control. Real-time shrinkage stress of investigated composites was measured using a tensometer; maximum shrinkage stress, stress rate (Rmax), and time to reach maximum stress rate (tmax) were recorded. Flexural strength and modulus were measured using a standard procedure, and curing efficiency of 4-mm long specimens was determined using bottom/top percentage Knoop microhardness. Data were analyzed using one-way analysis of variance and Bonferroni multiple range tests at a significance level of α=0.05. Results of shrinkage stress, Rmax, and tmax of all bulk-fill materials were significantly lower (p<0.05) than those of the control except for XF. All tested bulk-fill materials were able to achieve acceptable curing efficiency (≥80% bottom/top percentage) at 4-mm depth. In conclusion, this study reports a significant reduction in polymerization shrinkage stress while maintaining comparable curing efficiency at 4 mm for some bulk-fill composites and supports their potential use in posterior clinical situations.


1992 ◽  
Vol 70 (8) ◽  
pp. 716-719 ◽  
Author(s):  
K. J. Blessinger ◽  
G. Tunnicliff

3-Bromopyruvate inhibited 4-aminobutyrate aminotransferase (EC 2.6.1.19) from Pseudomonas fluorescens, apparently irreversibly. Kinetics of this inactivation were studied by continuously monitoring the enzyme reaction at 30 °C in the presence of inhibitor. Irrespective of how high an inhibitor concentration was present, a maximum rate of inactivation was eventually achieved (5.9 × 10−3 s−1), indicating the formation of a reversible inhibitor–enzyme complex before the final inactivation step. The dissociation constant of this complex was found to be 6.5 μM. This affinity labelling by 3-bromopyruvate suggests the presence of essential sulphydryl groups on the enzyme, since this compound is known to preferentially alkylate cysteinyl residues.Key words: 4-aminobutyrate, 4-aminobutyrate aminotransferase, inactivation, 3-bromopyruvate, affinity label, Pseudomonas fluorescens.


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