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. 1986 Jan;80(1):142-4.
doi: 10.1104/pp.80.1.142.

Purification to homogeneity of pyrroline-5-carboxylate reductase of barley

R Krueger  1 , H J Jäger, M Hintz, E Pahlich
Affiliations

Purification to homogeneity of pyrroline-5-carboxylate reductase of barley

R Krueger et al. Plant Physiol. 1986 Jan.

Abstract

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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