Purification and properties of two succinate semialdehyde dehydrogenases from human brain.

@article{Cash1978PurificationAP,
  title={Purification and properties of two succinate semialdehyde dehydrogenases from human brain.},
  author={Christopher D. Cash and Michel Maitre and Lucienne Ossola and Paul Mandel},
  journal={Biochimica et biophysica acta},
  year={1978},
  volume={524 1},
  pages={26-36}
}
In human brain there are two major isoenzymes of succinate semialdehyde dehydrogenase (succinate-semialdehyde: NAD+ oxidoreductase, EC 1.2.1.24). They are composed of two apparently identical subunits with a molecular weight of 69 000. The Km (limits) for their substrates NAD+ and succinate semialdehyde are 1.6.10(-5) M and 3.7.10(-6) M, respectively, for one enzyme, and 1.85.10(-5) M and 2.10(-6) M, respectively, for the other. These values, and other kinetic data obtained from the two enzymes… CONTINUE READING

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