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. 1975 Aug;56(2):259–262. doi: 10.1104/pp.56.2.259

Δ1-Pyrroline-5-carboxylic Acid Dehydrogenase in Barley, a Proline-accumulating Species 1

Samuel F Boggess a,2, Leslie G Paleg a, Donald Aspinall a
PMCID: PMC541800  PMID: 16659283

Abstract

The characteristics of the enzyme Δ1-pyrroline-5-carboxylic acid dehydrogenase from etiolated barley (Hordeum distichum) shoots have been examined. The bulk of the enzyme activity was found in the 10,000g pellet fraction, this activity being displayed only after detergent treatment of the suspended pellet. The enzyme was most active at pH 8, and activity was NAD-dependent. Enzyme activity was unaffected by either mannitol or sucrose in the reaction mixture up to a concentration of 0.45 m but was strongly inhibited by Cl− and, to a lesser extent, SO42−. The inhibition attributable to KCl was reversed by increasing the concentration of Δ1-pyrroline-5-carboxylic acid in the reaction mixture.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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