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Enzymatic properties of UFE,a novel marine fibrinolytic enzyme 被引量:3
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作者 WANG Dianliang LIU Wanshun HAN Baoqin 《Acta Oceanologica Sinica》 SCIE CAS CSCD 2007年第2期84-93,共10页
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... 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.Mn^2+ ,Cu^2+ and Fe^2+ ions were activators of UFE, while Fe^3+ and Ag^+ ions were inhibitors of UFE.Fe^2+ ion along with Fe^3+ 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. 展开更多
关键词 marine animal fibrinolytic enzyme protease enzyme properties
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