Azevedo, Ricardo A. and Smith, Richard J. and Lea, Peter J. (1992) Aspartate kinase regulation in maize: Evidence for co-purification of threonine-sensitive aspartate kinase and homoserine dehydrogenase. Phytochemistry, 31 (11). pp. 3731-3734.
Full text not available from this repository.Abstract
The threonine-sensitive and resistant forms of homoserine dehydrogenase activities were assayed in all fractions obtained during the purification of three aspartate kinase isoenzymes (threonine, lysine and lysine plus S-adenosylmethionine-sensitive) from maize cultures. The homoserine dehydrogenase isoenzyme resistant to inhibition by threonine, has a molecular weight of 70 000 and could be easily separated from the three aspartate kinase isoenzymes by ion-exchange chromatography and gel filtration; similarly the two lysine-sensitive forms of aspartate kinase could be separated from both forms of homoserine dehydrogenase. The homoserine dehydrogenase sensitive to threonine inhibition has a molecular weight of 180 000 and co-purified with the threonine-sensitive aspartate kinase isoenzyme. The hypothesis of the presence of a bifunctional protein containing activities of aspartate kinase-homoserine dehydrogenase is discussed.
| Item Type: | Article |
|---|---|
| Journal or Publication Title: | Phytochemistry |
| Uncontrolled Keywords: | Zea mays ; Gramineae ; aspartate kinase ; aspartic acid pathway ; homoserine dehydrogenase ; threonine. |
| Subjects: | G Geography. Anthropology. Recreation > GE Environmental Sciences |
| Departments: | Faculty of Science and Technology > Lancaster Environment Centre |
| ID Code: | 22735 |
| Deposited By: | ep_ss_importer |
| Deposited On: | 14 Jan 2009 13:21 |
| Refereed?: | No |
| Published?: | Published |
| Last Modified: | 26 Jul 2012 16:05 |
| Identification Number: | |
| URI: | http://eprints.lancs.ac.uk/id/eprint/22735 |
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