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. |
URL标识 | 查看原文 |
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
浏览0
下载0
收藏0
其他版本
除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。