Comparative study on conformational stability and subunit interactions of two bacterial asparaginases.

@article{Marlborough1975ComparativeSO,
  title={Comparative study on conformational stability and subunit interactions of two bacterial asparaginases.},
  author={David I. Marlborough and David Scott Miller and K A Cammack},
  journal={Biochimica et biophysica acta},
  year={1975},
  volume={386 2},
  pages={576-89}
}
The denaturation and reconstitution of Erwinia carotovora and Escherichia coli L-asparaginases has been followed by optical rotatory dispersion, circular dichroism and analytical ultracentrifugation. Denaturation in urea results in dissociation of the native enzyme (mol. wt. 140 000 approx.) to produce unfolded subunits (mol. wt. 35 000 approx.); the Erwinia L-asparaginase subunits can be refolded by dilution or dialysis in alkaline conditions, pH 10.5, without aggregation to the active… CONTINUE READING