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

Rolf Krueger | Zendy; HansJürgen Jäger | Zendy; Martin Hintz | Zendy; Edwin Pahlich | Zendy

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

Author(s) -

Rolf Krueger,

HansJürgen Jäger,

Martin Hintz,

Edwin Pahlich

Publication year - 1986

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.80.1.142

Subject(s) - proline dehydrogenase , proline , biochemistry , reductase , enzyme , dehydrogenase , chemistry , protein subunit , pyrroline , amino acid , biology , stereochemistry , gene

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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