A selective assay for prephenate aminotransferase activity in suspension-cultured cells of Nicotiana silvestris |
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Authors: | C. A. Bonner R. A. Jensen |
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Affiliation: | (1) Department of Microbiology and Cell Science, Institute of Food and Agricultural Sciences, University of Florida, 32611 Gainesville, FL, USA |
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Abstract: | Prephenate aminotransferase in Nicotiana silvestris Speg. et Comes is highly stable to thermal treatment. This property was exploited to obtain, by treatment at 70° C for 10 min, a residual level (1–4%) of aspartate aminotransferase activity that proved to be catalyzed exclusively by prephenate aminotransferase. The latter enzyme was the most mobile of all aspartate aminotransferase bands during polyacrylamide-gel electrophoresis conducted under non-denaturing conditions. This methodology for convenient assay of prephenate aminotransferase in crude extracts, as demonstrated for N. silvestris, may generally apply to higher plants since prephenate aminotransferase from a variety of plant sources has been found to exhibit high thermal stability.Abbreviations AGN L-arogenate - AT aminotransferase - ASP L-aspartate - GLU L-glutamate - HPP 4-hydroxyphenylpyruvate - 2-KG 2-ketoglutarate - OAA oxaloacetate - PPA prephenate - PPY phenylpyruvateFlorida Agricultural Experiment Station, Journal Series No. 8286 |
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Keywords: | Amino acids aromatic Aspartate aminotransferase font-variant:small-caps" >L-Arogenate Nicotiana (prephenate aminotransferase) Prephenate aminotransferase |
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