Abstract:
:A 36 kDa extracellular metalloprotease (designated to as vEP-MO6) was purified and characterized from Vibrio vulnificus sp. strain MO6 24/0. vEP-MO6 cleaved azocasein and a few other proteins such as prothrombin, plasminogen, fibrinogen and Factor Xa, which are associated with the blood coagulation pathway. The enzyme activity of vEP-MO6 was inhibited by EDTA, which was reversed by the addition of excess divalent cations. vEP-MO6 showed little or no activity toward various chromogenic substrates that are specific for other proteases. The cleavage of prothrombin by vEP-MO6 produced active thrombin, as revealed by an activity assay with thrombin-specific chromogenic substrate and Western blot analysis with anti-thrombin antibody. The enzyme also actively hydrolyzed fibrin polymer as well as the cross-linked fibrin. These results suggest that vEP-MO6 is a prothrombin-activating and cross-linked fibrin-degrading enzyme belonging to the metalloprotease family.
journal_name
Int J Mol Medjournal_title
International journal of molecular medicineauthors
Kwon JY,Chang AK,Park JE,Shin SY,Yoon SM,Lee JSsubject
Has Abstractpub_date
2007-01-01 00:00:00pages
157-63issue
1eissn
1107-3756issn
1791-244Xjournal_volume
19pub_type
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