Quaternary structure of higher plant glyceraldehyde-3-phosphate dehydrogenases.

@article{Cerff1979QuaternarySO,
  title={Quaternary structure of higher plant glyceraldehyde-3-phosphate dehydrogenases.},
  author={R{\"u}diger Cerff},
  journal={European journal of biochemistry},
  year={1979},
  volume={94 1},
  pages={243-7}
}
1. NAD(P)+-induced changes in the aggregational state of prepurified NADP-linked glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.13) were used to isolate the enzyme from Spinacia oleracea, Pisum sativaum and Hordeum vulgare. Each of the three plant species contains two separate isoenzymes. Isoenzyme 1 (fast moving during conventional electrophoresis) precipitates with the ammonium sulfate fraction 55--70% saturation. It shows two separate subunits in dodecylsulfate gels, which are probably… CONTINUE READING

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