Fresh carious and non-carious human dentine was crushed and the α-aminoacylpeptide hydrolase activity (EC 3.4.11) was quantitatively measured using N-L-aminoacyl-2-napthylamines of various amino acids as substrates. The activity per milligram protein in the sample in carious dentine was observed to be at least ten times higher than in non-carious coronal dentine. The difference was more pronounced (up to 500 times) when the rates of hydrolysis were calculated per milligram specimen. Active carious lesion revealed higher enzyme activity than arrested lesions, which difference was statistically significant. The values of arrested and residual carious lesions were on the level of those with fully formed root dentine. The values obtained from root dentine were about 5–10 times higher than in coronal dentine in living teeth. The rates of hydrolysis of the substrates catalyzed by enzymes from root dentine of teeth with gangrenous pulp or root-filled pulp chamber were nil or neglible. No significant difference could be demonstrated between permanent and deciduous teeth. The origin of these enzymes is thought to be the cellular components of the tissue while the more pronounced hydrolysis with carious dentine was thought to be microbial.

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