Subunit dissociations in natural and recombinant hemoglobins.

@article{Manning1996SubunitDI,
  title={Subunit dissociations in natural and recombinant hemoglobins.},
  author={Lois R Manning and W T Jenkins and John R Hess and Kim D. Vandegriff and Robert M. Winslow and James M. Manning},
  journal={Protein science : a publication of the Protein Society},
  year={1996},
  volume={5 4},
  pages={775-81}
}
A precise and rapid procedure employing gel filtration on Superose-12 to measure the tetramer-dimer dissociation constants of some natural and recombinant hemoglobins in the oxy conformation is described. Natural sickle hemoglobin was chosen to verify the validity of the results by comparing the values with those reported using an independent method not based on gel filtration. Recombinant sickle hemoglobin, as well as a sickle double mutant with a substitution at the Val-6(beta) receptor site… CONTINUE READING