Abstract
In order to characterize neutral proteases in gingiva, tissue specimens from periodontitis patients were subjected to different extraction procedures. In addition to collagenase and gelatinase, serine proteases having trypsin‐like and elastase‐like properties were detected by utilizing synthetic aminoacid substrates. High salt concentration was required for the optimal extraction of these enzymes. They also needed a certain ionic strength for their activity. The pH optimum for the trypsin‐like activity was 7.5 and for the elastase‐like activity 8.0. A synthetic plasmin substrate was also degraded by the extracts but no activity against native fibrin was found. These neutral proteases may play a significant part in the extracellular protein degradation in periodontium during inflammation.
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