L-amino acid oxidase from Trimeresurus jerdonii snake venom: purification, characterization, platelet aggregation-inducing and antibacterial effects.

Journal of natural toxins Pub Date : 2002-12-01
Qiu-Min Lu, Qin Wei, Yang Jin, Ji-Fu Wei, Wan-Yu Wang, Yu-Liang Xiong
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Abstract

An L-amino acid oxidase (LAO), designated as TJ-LAO, was purified to homogeneity from the venom of Trimeresurus jerdonii by Sephadex G-100 and Q Sepharose HP chromatography. The molecular weight of this enzyme was 110 kD as estimated by analytical gel filtration and was 55 kD by SDS-polyacrylamide gel electrophoresis, suggesting that the enzyme is composed of two subunits. The enzyme has an absorption spectrum characteristic of flavoproteins, containing 2 moles of FMN per mole of enzyme. The N-terminal sequence of TJ-LAO shares high homology with other viperid snake venom LAOs. Homology with elapid venom LAO is lower. TJ-LAO inhibited the growth of Escherichia coli, Staphylococcus aureus, Pseudomonas aeruginosa, and Bacillus megaterium. The antibacterial effect associated with LAO activity was elminated with the addition of catalase. Platelets in platelet-rich plasma aggregated upon the addition of TJ-LAO. The enzyme-induced aggregation was inhibited by catalase, suggesting formation of H2O2 was essential for TJ-LAO to induce platelet aggregation. These results showed H2O2 formation is important for the biological effects of LAO.

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大鼠蛇毒l -氨基酸氧化酶的纯化、鉴定、诱导血小板聚集及抑菌作用。
采用Sephadex G-100和Q Sepharose高效液相色谱法,从尖刺Trimeresurus jerdonii毒液中纯化出一种l -氨基酸氧化酶(L-amino acid oxidase, LAO),定名为TJ-LAO。经分析凝胶过滤测得该酶分子量为110 kD, sds -聚丙烯酰胺凝胶电泳测得该酶分子量为55 kD,表明该酶由两个亚基组成。该酶具有黄酮类蛋白的吸收光谱特征,每摩尔酶含有2摩尔FMN。TJ-LAO的n端序列与其他蛇毒lao具有高度同源性。与蛇毒LAO同源性较低。TJ-LAO抑制大肠杆菌、金黄色葡萄球菌、铜绿假单胞菌和巨芽孢杆菌的生长。过氧化氢酶的加入消除了与LAO活性相关的抗菌作用。富血小板血浆中的血小板在加入TJ-LAO后聚集。过氧化氢酶抑制了酶诱导的血小板聚集,表明H2O2的形成是TJ-LAO诱导血小板聚集所必需的。这些结果表明H2O2的形成对LAO的生物学效应很重要。
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