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短尾蝮蛇毒磷脂结合抗凝蛋白的酶学性质研究
Enzymatic characteristion of phospholipid-binding anticoagulation protein from Agkistrodon halys brevicaudus venom
【摘要】 目的:研究短尾蝮蛇毒磷脂结合抗凝蛋白(Phospholipid-binding anticoagulation protein,PBAP)的酶学性质。方法:通过对短尾蝮蛇毒PBAP精氨酸脂酶活性的测定,研究丝氨酸蛋白酶抑制剂苯甲基磺酰氟(Phenylmethanesulfonyl fluoride,PMSF)、胰蛋白酶、抑肽酶、二价金属离子(Ca2+、Mg2+、Co2+、Mn2+、Zn2+)、温度、pH、金属络合剂乙二胺四乙酸(Ethylene diamine tetraacetic acid,EDTA)对PBAP的影响。结果:丝氨酸蛋白酶抑制剂PMSF、胰蛋白酶对PBAP精氨酸酯酶有抑制作用,抑肽酶、Ca2+、Mg2+、Co2+、Mn2+、Zn2+、二胺四乙酸对PBAP精氨酸酯酶活性无明显影响,温度在20℃~90℃,pH在4.0~11.0的条件下,PBAP的精氨酸酯酶性质稳定。结论:丝氨酸蛋白酶抑制剂PMSF、胰蛋白酶对PBAP精氨酸酯酶有抑制作用,温度在20℃~90℃,pH在4.0~11.0的条件下,PBAP的精氨酸酯酶性质稳定。
【Abstract】 Objective:To study the enzymatic characteristics of phospholipid-binding anticoagulation protein(PBAP) from agkistrodon halys brevicaudus venom.Methods:The enzymatic characteristics of purified PBAP were studied by the effects of phenylmethanesulfonyl fluoride(PMSF),trypsin,aprotinin,bivalent metallic ion(Ca2+,Mg2+,Co2+,Mn2+,Zn2+),temperature,pH and ethylene diamine tetraacetic acid(EDTA) on PBAP.Results:PMSF and trypsin could inhibit the AEHE activity of PBAP. Aprotinin,bivalent metallic ion(Ca2+,Mg2+,Co2+,Mn2+,Zn2+)and EDTA had no effect on the AEHE activity of PBAP.The AEHE activity of PBAP was stable within 20℃~90℃ and pH4.0~11.0. Conclusion:PMSF and trypsin could inhibit the AEHE activity of PBAP.The AEHE activity of PBAP was stable within 20℃~90℃ and pH4.0~11.0.
【Key words】 Anticoagulation; Arginine ester hydrolysing enzyme; Enzymatic characterization;
- 【文献出处】 重庆医科大学学报 ,Journal of Chongqing Medical University , 编辑部邮箱 ,2010年11期
- 【分类号】Q55
- 【下载频次】62