Journalartikel

Jahr der Veröffentlichung: 1986

Seiten: 142-144

Zeitschrift: Plant Physiology

Bandnummer: 80

Heftnummer: 1

ISSN: 0032-0889

eISSN: 1532-2548

Open Access Status: Green

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

Verlag: 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-Zitierstil: 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-Zitierstil: 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