WANG Dianliang, LIU Wanshun, HAN Baoqin. Enzymatic properties of UFE, a novel marine fibrinolytic enzyme[J]. Acta Oceanologica Sinica, 2007, (2): 84-93.
Citation:
WANG Dianliang, LIU Wanshun, HAN Baoqin. Enzymatic properties of UFE, a novel marine fibrinolytic enzyme[J]. Acta Oceanologica Sinica, 2007, (2): 84-93.
WANG Dianliang, LIU Wanshun, HAN Baoqin. Enzymatic properties of UFE, a novel marine fibrinolytic enzyme[J]. Acta Oceanologica Sinica, 2007, (2): 84-93.
Citation:
WANG Dianliang, LIU Wanshun, HAN Baoqin. Enzymatic properties of UFE, a novel marine fibrinolytic enzyme[J]. Acta Oceanologica Sinica, 2007, (2): 84-93.
A novel potent protease, Urechis unicinctus fibrinolytic enzyme (UFE), was firstly discovered.The enzymatic properties of UFE were further investigated.As a low molecular mass protein, UFE appeared to be very stable to heat and pH.When temperature was below 50℃, the remnant enzyme activity remained almost unchanged, but when temperature was raised to 60℃, the remnant enzyme activity began to decrease rapidly.UFE was quite stable in the range of pH value from 3 to 12, especially in slightly alkaline pH value.Mn2+, Cu2+ and Fe2+ ions were activators of UFE, while Fe3+ and Ag+ ions were inhibitors of UFE.Fe2+ ion along with Fe3+ ion might regulate UFE activity in vivo.The optimum pH and temperature of UFE were about 8 and 50℃, respectively.Other characteristics of this enzyme were also studied.Systematic research results are significant when UFE is applied for medical and industrial purposes.