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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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Published in: | Plant and cell physiology 1987-07, Vol.28 (5), p.885-891 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that cite this one |
Online Access: | Get full text |
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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. |
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ISSN: | 0032-0781 1471-9053 |
DOI: | 10.1093/oxfordjournals.pcp.a077370 |