Isolation of a hemorrhagic toxin from the venom of Agkistrodon contortrix laticinctus (broad-banded copperhead) and pathogenesis of the hemorrhage induced by the toxin in mice |
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| Affiliation: | 1. Venom Evolution Lab, School of Biological Sciences, University of Queensland, St Lucia, QLD 4072, Australia;2. Division of Thrombosis and Hemostasis, Einthoven Laboratory for Vascular and Regenerative Medicine, Leiden University Medical Center, Albinusdreef 2, 2333 ZA Leiden, the Netherlands;3. Animal Ecology Lab, Department of Biology, Kyung Hee University, Seoul 130-701, Republic of Korea;1. National Laboratory for Development of Endangered Drug Resources in Northwest China, College of Life Sciences, Shaanxi Normal University, Xi''an, Shaanxi, 710062, China;2. Innovation Center for Qinba Regions Sustainable Development, College of Life Sciences, Shaanxi Normal University, Xi''an, Shaanxi, 710062, China;3. Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing, 100101, China;4. Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan;5. Institute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan;1. National Laboratory for Development of Endangered Drug Resources in Northwest China, College of Life Sciences, Shaanxi Normal University, Xi''an, Shaanxi, 710062, China;2. Innovation Center for Qinba region Stainable Development, College of Life Sciences, Shaanxi Normal University, Xi''an, Shaanxi, 710062, China;3. Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan;4. Institute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan |
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| Abstract: | - 1.1. A hemorrhagic toxin was isolated from the venom of Agkistrodon contortrix laticinctus (Broad-Banded Copperhead) by Sephacryl S-200 HR column chromatography followed by high performance chromatography on Waters DEAE 5PW and protein Pak 125 columns.
- 2.2. Homogeneity was determined by the presence of a single band in acrylamide gel electrophoresis with silver staining.
- 3.3. ACL hemorrhagic toxin I has a molecular weight of about 29,000, is slightly acidic, and is a metalloprotease with activity towards the substrates N,N-dimethylcasein and bovine fibrinogen. Although the toxin is able to hydrolyze fibrinogen in vitro, it does not possess any defibrinogenating activity in vivo whereas the crude venom does show this activity. It has similar cleavage specificities to other snake venom hemorrhagic toxins.
- 4.4. ACL hemorrhagic toxin I causes hemorrhage of rapid onset, present within 5 min of intramuscular injection into mice, and the pathogenesis is one of hemorrhage per rhexis in which capillary endothelial cells are ruptured.
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