Identification of human salivary protease activity toward mucin: Differences with caries

J. Piotrowski, A. Czajkowski, V. L.N. Murty, A. Slomiany, B. L. Slomiany

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


A protease activity directed toward high molecular weight salivary mucus glycoprotein was identified in the secretion of human submandibular salivary gland. The protease exhibited maximum activity at pH 7.0 - 7.4, and following ammonium sulfate fractionation yielded an active enzyme at 60% saturation which on SDS-PAGE gave 48 and 53 kDa protein bands. The enzyme exhibited serine-protease properties by showing susceptibility to phenyl methyl sulfonyl fluoride, α1-antitrypsin, and egg white and soybean inhibitors. The protease activity in submandibular saliva of caries-resistant subjects was found to be 3.8-fold greater than that in saliva of caries-susceptible individuals, thus suggesting that the enzyme expression may be linked to the resistance to caries.

Original languageEnglish (US)
Pages (from-to)939-947
Number of pages9
JournalBiochemistry International
Issue number5
StatePublished - 1992

All Science Journal Classification (ASJC) codes

  • Biochemistry


Dive into the research topics of 'Identification of human salivary protease activity toward mucin: Differences with caries'. Together they form a unique fingerprint.

Cite this