Stopped‐flow studies of the reaction of d‐tartronate semialdehyde‐2‐phosphate with human neuronal enolase and yeast enolase 1

@article{Brewer2010StoppedflowSO,
  title={Stopped‐flow studies of the reaction of d‐tartronate semialdehyde‐2‐phosphate with human neuronal enolase and yeast enolase 1},
  author={J. Brewer and Jared S McKinnon and R. Phillips},
  journal={FEBS Letters},
  year={2010},
  volume={584}
}
We determined the kinetics of the reaction of human neuronal enolase and yeast enolase 1 with the slowly‐reacting chromophoric substrate d‐tartronate semialdehyde phosphate (TSP), each in tris (tris (hydroxymethyl) aminomethane) and another buffer at several Mg2+ concentrations, 50 or 100 μM, 1 mM and 30 mM. All data were biphasic, and could be satisfactorily fit, assuming either two successive first‐order reactions or two independent first‐order reactions. Higher Mg2+ concentrations reduce the… Expand
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