Journal article

Publication year: 1986

Pages: 142-144

Journal: Plant Physiology

Volume number: 80

Issue number: 1

ISSN: 0032-0889

eISSN: 1532-2548

Open access status: Green

DOI Link: https://doi.org/10.1104/pp.80.1.142

Publisher: Oxford University Press

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.

Harvard Citation style: KRUEGER, R., JAGER, H., HINTZ, M. and PAHLICH, E. (1986) PURIFICATION TO HOMOGENEITY OF PYRROLINE-5-CARBOXYLATE REDUCTASE OF BARLEY, Plant Physiology, 80(1), pp. 142-144. https://doi.org/10.1104/pp.80.1.142

APA Citation style: KRUEGER, R., JAGER, H., HINTZ, M., & PAHLICH, E. (1986). PURIFICATION TO HOMOGENEITY OF PYRROLINE-5-CARBOXYLATE REDUCTASE OF BARLEY. Plant Physiology. 80(1), 142-144. https://doi.org/10.1104/pp.80.1.142