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Matsuzawa, T.

Purification and characterization of pyrroline-5-carboxylate reductase from bovine retina.

Bovine retinal pyrroline-5-carboxylate reductase (L-proline: NAD(P)+ 5-oxidoreductase, EC 1.5.1.2) was purified 180-fold from crude extract, using affinity chromatography with 2',5'-ADP Sepharose 4B. The purified enzyme utilized either NADH or NADPH as the coenzyme. The enzyme activity was inhibited with ATP, and activated with potassium and phosphate ions, suggesting that it may be regulated by the energy level and the redox state in the retina. The distribution of this enzyme in bovine lens suggests a developmental trail of the enzyme in the lens.[1]

References

Purification and characterization of pyrroline-5-carboxylate reductase from bovine retina. Matsuzawa, T. Biochim. Biophys. Acta (1982) [Pubmed]

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