Catalase/peroxidase activity in dental pulp.
Extrinsic stains on vital teeth are bleached with 30% hydrogen peroxide (H2O2) or carbamide peroxide, H2O2 greatly inhibits the activity of several enzymes. Free H2O2 and carbamide peroxide readily enter the pulp through the coronal wall of the tooth. Nevertheless, adverse effects have been remarkably rare. This study was undertaken to determine whether dental pulp exhibits any catalase or peroxidase activity that might protect it from damage during vital bleaching procedures. Pulpal tissue from healthy human teeth was assayed for catalase and glutathione peroxidase activity. A phosphate buffer extract of the tissue served as the source of the enzymes. The rate of breakdown of H2O2 by the tissue extract was measured and the rate constant for catalase was determined. The catalase activity, defined as microM H2O2 broken down/min/mg wet tissue, was determined and found to be only 2 x 10(-2), which is very low. The fibrous pulpal tissue was found to exhibit virtually no glutathione peroxidase activity.
Bowles
W H
WH
Department of Biochemistry, Baylor College of Dentistry, Dallas, TX.
Burns
H
H
D002374:Catalase / Q000378:metabolism; D003782:Dental Pulp / Q000201:enzymology*; D005979:Glutathione Peroxidase / Q000378:metabolism*; D006801:Humans; D006861:Hydrogen Peroxide / Q000378:metabolism*; D014073:Tooth Bleaching
D006861:Hydrogen Peroxide; D002374:Catalase; D005979:Glutathione Peroxidase