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A selective assay for prephenate aminotransferase activity in suspension-cultured cells ofNicotiana silvestris

✍ Scribed by C. A. Bonner; R. A. Jensen

Publisher: Springer-Verlag
Year: 1987
Tongue: English
Weight: 846 KB
Volume: 172
Category: Article
ISSN: 0032-0935
DOI: 10.1007/bf00398672

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✦ Synopsis

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 rain, 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.

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