Enzymatic characteristion of phospholipid-binding anticoagulation protein from Agkistrodon halys brevicaudus venom

LI Yuan-hong; et al

doi:10.13406/j.cnki.cyxb.2010.11.002

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Enzymatic characteristion of phospholipid-binding anticoagulation protein from Agkistrodon halys brevicaudus venom

更新时间：2024-01-17

- Enzymatic characteristion of phospholipid-binding anticoagulation protein from Agkistrodon halys brevicaudus venom
- Journal of Chongqing Medical University Vol. 35, Issue 11, Pages: 1639-1641(2010)
- 作者机构：
  
  1. 广西医科大学第一附属医院药剂科
  2. 广西医科大学蛇毒研究所
- 作者简介：
- 基金信息：
- DOI：10.13406/j.cnki.cyxb.2010.11.002
  CLC： Q55
- Published：2010，
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[1]黎渊弘,罗艳萍,廖共山.短尾蝮蛇毒磷脂结合抗凝蛋白的酶学性质研究[J].重庆医科大学学报,2010,35(11):1639-1641.

LI Yuan-hong, et al. Enzymatic characteristion of phospholipid-binding anticoagulation protein from Agkistrodon halys brevicaudus venom. [J]. Journal of Chongqing Medical University 35(11):1639-1641(2010)
[1]黎渊弘,罗艳萍,廖共山.短尾蝮蛇毒磷脂结合抗凝蛋白的酶学性质研究[J].重庆医科大学学报,2010,35(11):1639-1641. DOI： 10.13406/j.cnki.cyxb.2010.11.002.

LI Yuan-hong, et al. Enzymatic characteristion of phospholipid-binding anticoagulation protein from Agkistrodon halys brevicaudus venom. [J]. Journal of Chongqing Medical University 35(11):1639-1641(2010) DOI： 10.13406/j.cnki.cyxb.2010.11.002.

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.

关键词

抗凝蛋白精氨酸酯酶酶学性质

Keywords

AnticoagulationArginine ester hydrolysing enzymeEnzymatic characterization

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