Related Experiment Video
Updated: Oct 3, 2026
Large-Scale Purification of Porcine or Bovine Photoreceptor Outer Segments for Phagocytosis Assays on Retinal Pigment Epithelial Cells
Published on: December 12, 2014
Purification and characterization of pyrroline-5-carboxylate reductase from bovine retina
Abstract:
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.
More Related Videos
09:19Strategic Screening and Characterization of the Visual GPCR-mini-G Protein Signaling Complex for Successful Crystallization
Published on: March 16, 2020
11:08Two Peeling Methods for the Isolation of Photoreceptor Cell Compartments in the Mouse Retina for Protein Analysis
Published on: December 7, 2021