Neurotoxic activity of Gln49 phospholipase A2 from Gloydius ussuriensis snake venom
β Scribed by Yan Chang; Yingxue Li; Yongming Bao; Lijia An
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 298 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0260-437X
- DOI
- 10.1002/jat.1222
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β¦ Synopsis
A novel neurotoxic protein phospholipase A 2 (PLA 2 ), molecular weight 13 881.83 Da, has been isolated from snake venom of Gloydius ussuriensis, named as Gln49-PLA 2 , which shows weak lethal toxic, myotoxic and apparent anticoagulant activity, but lacks phospholipase activity. The Gln49-PLA 2 obviously induced an increase of the pain threshold in intoxicated 615 mice compared with the control group, suggesting it is a neurotoxin. Hot-plate tests also showed that its analgesic activity was dose-dependent, and naloxone antagonized the analgesic effect, implying the mechanism of action of Gln49-sPLA 2 is correlated with opioid receptors. Electrophysiology studies revealed decreases in the action potential and the nerve conduction velocity in isolated hoptoad (Bufo bufo gargarizans Cantor) sciatic nerve, indicating Gln49-PLA 2 most probably had effects on ion channels.
π SIMILAR VOLUMES
Basic proteins I and I1 (BP-I and BP-11) isolated from Tnmeresurusflavoviridis venom, which are classified into a group of lysine-49-phospholipases A2 (Lys-49-PLA3, exhibited only limited lipolytic activity for the mixed micelles of various phospholipids. Based on the finding that BP-11 elicits a st
Trimeresurus fivoviridis (Habu snake) venom aspartate-49-phospholipase A2 (Asp-49-PLAz) was reacted at pH 9.0 with a 2-fold molar excess of 2,4,6-trinitrobenzenesdfonate in the absence of Ca" and two trinitrophenylated derivatives were isolated by HPLC. One was a derivative modified at Lys-11 and it