Ligand binding properties and structural studies of recombinant and chemically modified hemoglobins altered at beta 93 cysteine.

@article{Cheng2002LigandBP,
  title={Ligand binding properties and structural studies of recombinant and chemically modified hemoglobins altered at beta 93 cysteine.},
  author={Yi Xin Cheng and Tong-Jian Shen and Virgil Simplaceanu and Chien Ho},
  journal={Biochemistry},
  year={2002},
  volume={41 39},
  pages={
          11901-13
        }
}
To investigate the roles of beta93 cysteine in human normal adult hemoglobin (Hb A), we have constructed four recombinant mutant hemoglobins (rHbs), rHb (betaC93G), rHb (betaC93A), rHb (betaC93M), and rHb (betaC93L), and have prepared two chemically modified Hb As, Hb A-IAA and Hb A-NEM, in which the sulfhydryl group at beta93Cys is modified by sulfhydryl reagents, iodoacetamide (IAA) and N-ethylmaleimide (NEM), respectively. These variants at the beta93 position show higher oxygen affinity… CONTINUE READING

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