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Type: Journal article
Title: Interference with the citrulline-based nitric oxide synthase assay by argininosuccinate lyase activity in Arabidopsis extracts
Author: Tischner, R.
Galli, M.
Heimer, Y.
Bielefeld, S.
Okamoto, M.
Mack, A.
Crawford, N.
Citation: The Federation of European Biochemical Societies (FEBS) Journal, 2007; 274(16):4238-4245
Publisher: Blackwell Publishing Ltd
Issue Date: 2007
ISSN: 1742-464X
Statement of
Rudolf Tischner, Mary Galli, Yair M. Heimer, Sarah Bielefeld, Mamoru Okamoto, Alyson Mack and Nigel M. Crawford
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, 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.
Keywords: Arabidopsis
argininosuccinate lyase
nitric oxide
DOI: 10.1111/j.1742-4658.2007.05950.x
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