中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Purification, characterization and biological activities of the L-amino acid oxidase from Bungarus fasciatus snake venom

文献类型:期刊论文

作者Wei JF1,3; Yang HW1; Wei XL3; Qiao LY3; Wang WY2; He SH*1,3; weijifu@hotmail.com; shoahenghe@ hotmail.com
刊名TOXICON
出版日期2009
卷号54期号:3页码:262-271
关键词L-amino Acid Oxidases Bungarus Fasciatus Myonecrosis Apoptosis Inflammation
ISSN号0041-0101
英文摘要L-Amino acid oxidases (LAAOs) are widely distributed in snake venoms, which contribute to the toxicity of venoms. However, LAAO from Bungarus fasciatus (B. fasciatus) snake venom has not been isolated previously. In the present study, LAAO from B. fasciatus snake venom was purified by SP-Sepharose HP anion exchange chromatography followed by Heparin-Sepharose FF affinity chromatography procedure and the purified enzyme was named BF-LAAO. BF-LAAO presented an estimated molecular weight of 55 kDa in SDS-PAGE and an apparent molecular weight of 70 kDa in size-exclusion chromatography suggesting that BF-LAAO is a monomeric protein. Kinetics studies showed that BF-LAAO was very active against L-Tyr, L-Asp, L-Phe, L-Glu, L-Trp, L-His, L-Gln, L-Ile, L-Met, L-Leu and moderately active against L-Lys, L-Arg, L-Ala and L-Asn. BF-LAAO exhibited a cytotoxic effect on A549 cells and caused up to 41.2% apoptosis of A549 cells following 12 h incubation period. In the mouse peritoneum, BF-LAAO provoked a marked increase in the number of neutrophils, lymphocytes and macrophages following injection. It also induced rabbit platelet aggregation in a dose-dependent manner. At 3 h following injection, BF-LAAO elicited severe inflammation in the gastrocnemius muscles of mice, but failed to induce significant organ damage. In conclusion, the cytotoxic and proinflammatory activities of BF-LAAO could be the main cause of the local inflammation, which helps us to understand the pathogenesis of snakebite.
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语种英语
资助机构This project was sponsored by the Major State Basic Research Program of China (973 Program) (No. 2007CB512400) and the National Natural Science Foundation of China (No. 30801016, 30570813, 30772032). ; This project was sponsored by the Major State Basic Research Program of China (973 Program) (No. 2007CB512400) and the National Natural Science Foundation of China (No. 30801016, 30570813, 30772032). ; This project was sponsored by the Major State Basic Research Program of China (973 Program) (No. 2007CB512400) and the National Natural Science Foundation of China (No. 30801016, 30570813, 30772032). ; This project was sponsored by the Major State Basic Research Program of China (973 Program) (No. 2007CB512400) and the National Natural Science Foundation of China (No. 30801016, 30570813, 30772032).
公开日期2010-08-24
源URL[http://159.226.149.42:8088/handle/152453/5391]  
专题昆明动物研究所_其他
通讯作者weijifu@hotmail.com; shoahenghe@ hotmail.com
作者单位1.Clinical Research Centre, The First Affiliated Hospital of Nanjing Medical University, Nanjing, Jiangsu 210029, China
2.Department of Animal Toxicology, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, Yunnan 650223, China
3.Allergy and Inflammation Research Institute, The Shantou University Medical College, Shantou, Guangdong 515031, China
推荐引用方式
GB/T 7714
Wei JF,Yang HW,Wei XL,et al. Purification, characterization and biological activities of the L-amino acid oxidase from Bungarus fasciatus snake venom[J]. TOXICON,2009,54(3):262-271.
APA Wei JF.,Yang HW.,Wei XL.,Qiao LY.,Wang WY.,...&shoahenghe@ hotmail.com.(2009).Purification, characterization and biological activities of the L-amino acid oxidase from Bungarus fasciatus snake venom.TOXICON,54(3),262-271.
MLA Wei JF,et al."Purification, characterization and biological activities of the L-amino acid oxidase from Bungarus fasciatus snake venom".TOXICON 54.3(2009):262-271.

入库方式: OAI收割

来源:昆明动物研究所

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