Oral Medicine
Fusobacterium nucleatum serine protease identified
Published in Drug Week, June 25th, 2004
In a recent study from Israel, a "65 kDa protease was partially purified from extracellular vesicles of Fusobacterium nucleatum cultures by preparative SDS-PAGE followed by electroelution."
"The pH optimum of the protease is 7.5-8.0 and its activity could be inhibited by serine protease inhibitors," reported G. Bachrach and coauthors at the Hebrew University of Jerusalem.
"The protease was found to degrade the extracellular matrix proteins fibrinogen and fibronectin as well as collagen I and collagen IV, which were degraded at 37 degree C...
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Source: Drug Week (2004-06-25)
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