ISOLATION AND CHARACTERIZATION OF A METALLOPROTEINASE WITH WEAK HEMORRHAGIC ACTIVITY FROM THE VENOM OF THE SNAKE BOTHROPS-ASPER (TERCIOPELO)
ISOLATION AND CHARACTERIZATION OF A METALLOPROTEINASE WITH WEAK HEMORRHAGIC ACTIVITY FROM THE VENOM OF THE SNAKE BOTHROPS-ASPER (TERCIOPELO)
复制标题
DOI：
10.1016/0041-0101(94)00138-x
复制
发表时间：
1995-01-01
期刊：
影响因子：
2.8
通讯作者：
OVADIA, M
中科院分区：
文献类型：
--
作者：
GUTIERREZ, JM;ROMERO, M;OVADIA, M
采用CM-Sephadex离子交换层析和Sephacryl S-200凝胶过滤，从哥斯达黎加（太平洋地区）Bothrops asper毒液中纯化出一种金属蛋白酶BaP1。这种酶有一个mel。含有少量的Cys和大量的Asp、Leu、Ser和Glu。BaP1水解酪蛋白、皮粉蓝和纤维蛋白原，最佳pH为8.0。它迅速消化纤维蛋白原的A -链，然后是B -链，而γ -链不受影响。螯合剂（EDTA和1,10-菲罗啉）抑制蛋白水解活性，而2-巯基乙醇和大豆胰蛋白酶抑制剂对蛋白水解活性没有影响。BaP1出血性较弱，最低出血性剂量为20 μ g；该活性被EDTA抑制，并在60℃孵育后消失。此外，BaP1诱导水肿和轻度肌毒作用，缺乏凝血、去纤和致死作用。
A metalloproteinase, named BaP1, was purified to homogeneity from the venom of Bothrops asper (Pacific region) of Costa Rica by ion-exchange chromatography on CM-Sephadex and gel filtration on Sephacryl S-200. The enzyme has a mel. wt of 24,000 and contains few Cys and high numbers of Asp, Leu, Ser and Glu. BaP1 hydrolyzes casein, hide powder azure and fibrinogen, having an optimal pH of 8.0. It rapidly digests the A alpha-chain of fibrinogen and, later on, the B beta-chain, leaving the gamma-chain unaffected. Chelating agents (EDTA and 1,10-phenanthroline) inhibited proteolytic activity, whereas 2-mercaptoethanol and soybean trypsin inhibitor did not affect this activity. BaP1 has a weak hemorrhagic activity, with a minimum hemorrhagic dose of 20 mu g; this activity was inhibited by EDTA and was abolished after incubation at 60 degrees C. In addition, BaP1 induces edema and a mild myotoxic effect, lacking coagulant, defibrinating and lethal effects.