Hemoglobin providence. Functional consequences of two alterations of the 2,3-diphosphoglycerate binding site at position beta 82.

@article{Bonaventura1976HemoglobinPF,
  title={Hemoglobin providence. Functional consequences of two alterations of the 2,3-diphosphoglycerate binding site at position beta 82.},
  author={Joseph Bonaventura and Celia Bonaventura and Bolling Sullivan and Guido Ferruzzi and Paul R. Mccurdy and Jack J. Fox and Winston F. Moo-Penn},
  journal={The Journal of biological chemistry},
  year={1976},
  volume={251 23},
  pages={
          7563-71
        }
}
Position beta 82 in human hemoglobin (Hb) is normally occupied by lysine, a positively charged residue that is involved in the binding of anionic cofactors. This residue is substituted by a neutral residue in Hb Providence Asn and by a negatively charged residue in Hb Providence Asp. Hb Providence Asp shows more differences from Hb A than does Hb Providence Asn in studies of the kinetics and equilibria of ligand binding. For both forms, homotropic (cooperative) interactions are normal with n… CONTINUE READING

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