来自极北蝰毒液中一种激肽原的纯化及特性研究
Purification and properties of a kininogenin from the venom of Vipera ammodytes ammodytes.
作者信息
Bailey G S, Shipolini R A
出版信息
Biochem J. 1976 Feb 1;153(2):409-14. doi: 10.1042/bj1530409.
A kininogenin (EC 3.4.21.8) was purified from the venom of Vipera ammodytes ammodytes (European sand viper) by a combination of gel filtration and ion-exchange chromatography. The enzyme is approximately six times more active than bovine trypsin in its ability to release vasoactive peptides from a plasma precursor. The kininogenin is a glycoprotein containing 18-20% by weight of carbohydrate. It showed a mol. wt. of 40500 on gel filtration. Gel electrophoresis of the reduced sample in the presence of sodium dodecyl sulphate and 2-mercaptoethanol revealed the presence of two major components of mol.wt. 34300 and 31300. The heterogeneity, which was also observed on disc electrophoresis, was removed by incubation with neuraminidase. After incubation with neuraminidase the kininogenin retained full enzymic activity and possessed an isoelectric point of pH7.2. The carbohydrate content has been decreased to 10% by weight, and the single component seen on electrophoresis in the presence of sodium dodecyl sulphate and 2-mercaptoethanol corresponded to a mol.wt. of 29500.
通过凝胶过滤和离子交换色谱相结合的方法，从欧洲蝰蛇（Vipera ammodytes ammodytes）的毒液中纯化出一种激肽原酶（EC 3.4.21.8）。该酶从血浆前体释放血管活性肽的能力约为牛胰蛋白酶的六倍。激肽原酶是一种糖蛋白，碳水化合物含量占其重量的18 - 20%。凝胶过滤显示其分子量为40500。在十二烷基硫酸钠和2-巯基乙醇存在下对还原样品进行凝胶电泳，结果显示存在分子量分别为34300和31300的两个主要组分。在圆盘电泳中也观察到了这种异质性，用神经氨酸酶孵育可消除这种异质性。用神经氨酸酶孵育后，激肽原酶保留了全部酶活性，其等电点为pH7.2。碳水化合物含量已降至占重量的10%，在十二烷基硫酸钠和2-巯基乙醇存在下电泳观察到的单一成分对应分子量为29500。
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