Localization and properties of hydroxypyruvate and glyoxylate reductases in spinach leaf particles.

@article{Tolbert1970LocalizationAP,
  title={Localization and properties of hydroxypyruvate and glyoxylate reductases in spinach leaf particles.},
  author={N. E. Tolbert and Russell K. Yamazaki and A. Oeser},
  journal={The Journal of biological chemistry},
  year={1970},
  volume={245 19},
  pages={5129-36}
}
A NADH-hydroxypyruvate reductase was located in peroxisomes isolated from spinach leaves. The enzyme was precipitated by between 15 to 23 g of (NH4)$04 per 100 ml and had a pH optimum at 6.4. It was also akive with NADPH at a pH optimum of 5.1, and the NADH:NADPH ratio of maximum activity was about 13:l. The reductase with either NADH or NADPH was about 4.3-fold more active with hydroxypyruvate than with glyoxylate. Through separation of proteins by electrofocusing, by Sephadex 6200 column… CONTINUE READING
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ARMY, (Editors), Harvesting the sun

  • A. SAN PIETRO, F. A. GREER, J T.
  • 1967

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