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Measurement of serine acetyltransferase activity in crude plant extracts by a coupled assay system using cysteine synthase

Serine acetyltransferase (SATase) (EC 2.3.1.30) catalyzes the formation of Oacetyl-L-serine (OAS) from L-serine in the presence of acetyl-CoA. A novel assay method was developed for measuring this enzyme activity in extracts from plant tissues. The assay consists of a coupled system in which the OAS...

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Bibliographic Details
Published in:Plant and cell physiology 1987-07, Vol.28 (5), p.885-891
Main Authors: Nakamura, K. (Chiba Univ., Matsudo (Japan). Faculty of Horticulture), Hayama, A, Masada, M, Fukushima, K, Tamura, G
Format: Article
Language:English
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Summary:Serine acetyltransferase (SATase) (EC 2.3.1.30) catalyzes the formation of Oacetyl-L-serine (OAS) from L-serine in the presence of acetyl-CoA. A novel assay method was developed for measuring this enzyme activity in extracts from plant tissues. The assay consists of a coupled system in which the OAS formed is converted to cysteine by the addition of cysteine synthase (CSase) (EC 4.2.99.8). Cysteine thus formed is determined colorimetrically and serves as a measure for SATase activity. This method is rapid, simple and sensitive, and can be readily adapted for measurement of SATase activity in crude tissue extracts or homogenates.
ISSN:0032-0781
1471-9053
DOI:10.1093/oxfordjournals.pcp.a077370