Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 80:142-144 (1986)
© 1986 American Society of Plant Biologists

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Articles

Purification to Homogeneity of Pyrroline-5-Carboxylate Reductase of Barley

Rolf Krueger, Hans-Jürgen Jäger, Martin Hintz and Edwin Pahlich

Institut für Pflanzenphysiologie der Justus-Liebig-Universität Giessen, D-6300 Giebetaen, Federal Republic of Germany, Institut für Produktions- und Ökotoxikologie der Bundesforschungsanstalt für Landwirtschaft, D-3300 Braunschweig, Federal Republic of Germany

An enzyme has been purified to homogeneity from barley seedlings which has `proline dehydrogenase' and the pyrroline-5-carboxylic acid reductase activities. The purification achieved is 39,000-fold as calculated from the proline dehydrogenase activity. The subunit molecular weight of the protein is 30 kilodaltons. The native enzyme has molecular weights up to 480 kilodaltons, depending on the buffer environment. From the pH profiles, the specific activities and thermodynamic considerations, it is concluded that the plant proline dehydrogenase functions in vivo as a pyrroline-5-carboxylate reductase.




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Home page
 Plant Cell PhysiolHome page
M. Murahama, T. Yoshida, F. Hayashi, T. Ichino, Y. Sanada, and K. Wada
Purification and Characterization of {Delta}1-Pyrroline-5-Carboxylate Reductase Isoenzymes, Indicating Differential Distribution in Spinach (Spinacia oleracea L.) Leaves
Plant Cell Physiol., July 1, 2001; 42(7): 742 - 750.
[Abstract] [Full Text] [PDF]


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Copyright © 1986 by the American Society of Plant Biologists