Vibrio extracellular protease with prothrombin activation and fibrinolytic activities.
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.
Kwon
Ju Young
JY
Research Center for Proteineous Materials, Chosun University, Gwangju 501-759, Korea.
Chang
Alan K
AK
Park
Jung Eun
JE
Shin
Song Yub
SY
Yoon
Seong Myeong
SM
Lee
Jung Sup
JS
D000595:Amino Acid Sequence; D002614:Chelating Agents / Q000494:pharmacology; D004789:Enzyme Activation; D005337:Fibrin / Q000378:metabolism; D005342:Fibrinolysis; D045726:Metalloproteases / Q000037:antagonists & inhibitors / Q000235:genetics / Q000302:isolation & purification / Q000502:physiology*; D008670:Metals / Q000494:pharmacology; D008969:Molecular Sequence Data; D011480:Protease Inhibitors / Q000494:pharmacology; D011516:Prothrombin / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D041261:Vibrio vulnificus / Q000201:enzymology* / Q000235:genetics
D002614:Chelating Agents; D008670:Metals; D011480:Protease Inhibitors; D011516:Prothrombin; D005337:Fibrin; D045726:Metalloproteases