Characterization of a membrane bound protease from an aggressive periodontal pathogen, Tannerella forsythia, was carried out by incubating isolated enzyme with highly fluorescein-labeled gelatin.  Enzymatic cleavage of the fluorescein-labeled gelatin resulted in relief of fluorescent quenching and an increase in relative fluorescence.  Kinetic parameters, Vmax and Km, were calculated for the enzyme using this assay. It was additionally shown that enzyme activity was inhibited by metalloproteinase inhibitor, 1,10-phenanthroline, in a dose-dependent manner.  Km and Vmax were also determined for the enzyme in the presence of 1,10-phenanthroline.

Enzyme kinetic analysis of a newly isolated protease from periodontal pathogen, <i>Tannerella forsythia</i>

243rd National Meeting (2012)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.

Enzyme kinetic analysis of a newly isolated protease from periodontal pathogen, Tannerella forsythia