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Characterization of human salivary β‐N‐acetyl‐ D‐glucosaminidase (NAGase)
Author(s) -
FOUDA NASSER ELTOUKHY,
SÖDER PERÖSTEN,
OLSSON MARIELOUISE
Publication year - 1988
Publication title -
european journal of oral sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.802
H-Index - 93
eISSN - 1600-0722
pISSN - 0909-8836
DOI - 10.1111/j.1600-0722.1988.tb01555.x
Subject(s) - saliva , chemistry , enzyme assay , salivary proteins , enzyme , food science , biochemistry
– NAGase activity was studied in mixed whole, parotid, and submandibular saliva. The maximum activity of NAGase was found to be at pH 5.0. NAGase activity varied considerably among the subjects. The data indicated that a large portion of NAGase activity originates from oral microorganisms. NAGase activity was greatly reduced after heating for 45 min at 50 °C. The residual activity after storage at – 20°C was higher than the original activity. The enzyme activity was markedly diminished after the addition of Sn ++ and Ag + ions, while no activity was detected after the addition of Hg + ion.