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- W1570517718 abstract "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 microM), 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." @default.
- W1570517718 created "2016-06-24" @default.
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- W1570517718 date "2007-07-25" @default.
- W1570517718 modified "2023-10-07" @default.
- W1570517718 title "Interference with the citrulline-based nitric oxide synthase assay by argininosuccinate lyase activity in<i>Arabidopsis</i>extracts" @default.
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- W1570517718 doi "https://doi.org/10.1111/j.1742-4658.2007.05950.x" @default.
- W1570517718 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17651442" @default.
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