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Method for determination of invertase acitivity in homogentes of human dental plaque
Author(s) -
FIEHN NILSERIK,
MOE DENNIS
Publication year - 1981
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.1600-0722.1981.tb01708.x
Subject(s) - invertase , dental plaque , dentistry , medicine , orthodontics , chemistry , biochemistry , enzyme
– Supragingival human dental plaque was ecllected from patients with evidence of caries. The plaque was frozen and stored at‐20°C. Pooled plaque was homogenized in acelate buffer pH 5.0 in an ice‐water bath. By incubating the homogenate at pH 5.0 with [U‐°C]‐sucrose the formation fo glucose and fructose was followed. Incubation in acetate buffer at pH 5.0 eliminated the glycosyltransferase activities adn teh glycolytic pathway. Normal Michaclis‐Menten kinetics were observed until about 40 mM sucrose. At highert concentration of sucrose, excess substrate inhibition occurred. Storage of the homogenate at −20° C resulted in decrease of the invertase activity with time.