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首页> 外文期刊>The FEBS journal >Interference with the citrulline-based nitric oxide synthase assay by argininosuccinate lyase activity in Arabidopsis extracts
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Interference with the citrulline-based nitric oxide synthase assay by argininosuccinate lyase activity in Arabidopsis extracts

机译：拟南芥提取物中精氨酸琥珀酸裂合酶活性干扰瓜氨酸基一氧化氮合酶测定

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摘要

There are many reports of an arginine-dependent nitric oxide synthase activity in plants; however, the gene(s) or protein(s) responsible for this activity have yet to be convincingly identified. To measure nitric oxide synthase activity, many studies have relied on a citrulline-based assay that measures the formation of l-citrulline from l-arginine using ion exchange chromatography. In this article, we report that when such assays are used with protein extracts from Arabidopsis, an arginine-dependent activity was observed, but it produced a product other than citrulline. TLC analysis identified the product as argininosuccinate. The reaction was stimulated by fumarate (> 500 μm), implicating the urea cycle enzyme argininosuccinate lyase (EC 4.3.2.1), which reversibly converts arginine and fumarate to argininosuccinate. These results indicate that caution is needed when using standard citrulline-based assays to measure nitric oxide synthase activity in plant extracts, and highlight the importance of verifying the identity of the product as citrulline.
机译：关于植物中精氨酸依赖性一氧化氮合酶活性的报道很多。然而，尚未令人信服地鉴定出负责该活性的基因或蛋白质。为了测量一氧化氮合酶活性，许多研究依赖于基于瓜氨酸的测定，该测定使用离子交换色谱法测量从1-精氨酸中形成1-瓜氨酸。在本文中，我们报告说，当这种测定法与拟南芥的蛋白提取物一起使用时，观察到精氨酸依赖性活性，但产生的产物不是瓜氨酸。 TLC分析鉴定该产物为精氨酸琥珀酸酯。富马酸酯（> 500μm）刺激了反应，牵涉尿素循环酶精氨酸琥珀酸酯裂解酶（EC 4.3.2.1），该酶可逆地将精氨酸和富马酸酯转化为精氨酸琥珀酸酯。这些结果表明，在使用基于瓜氨酸的标准测定法来测量植物提取物中一氧化氮合酶活性时需要谨慎，并强调了验证产品身份为瓜氨酸的重要性。

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