Purification and characterization of the recombinant human aldose reductase expressed in baculovirus system.

@article{Nishimura1991PurificationAC,
  title={Purification and characterization of the recombinant human aldose reductase expressed in baculovirus system.},
  author={Chiaki Nishimura and Takashi Yamaoka and Makoto Mizutani and Koichiro Yamashita and Tai Akera and Tsuyoshi Tanimoto},
  journal={Biochimica et biophysica acta},
  year={1991},
  volume={1078 2},
  pages={171-8}
}
Large quantities of recombinant human aldose reductase were produced using Spodoptera frugiperda cells and properties of the enzyme were characterized. Direct purification of the recombinant aldose reductase by affinity column chromatography using Matrex gel orange A yielded a single 36 kDa band, similar in size to the purified human muscle aldose reductase, on a sodium dodecyl sulfate-polyacrylamide gel after silver staining. The isoelectric point of the recombinant enzyme was 5.85 which is… CONTINUE READING