Laboratory Experiments

Experiment 18 Haemoglobin — Oxygenation, and Magnetic and Spectroscopic Studies
  • Ei-Ichiro Ochiai
  • David R. Williams


Haemoglobin is the oxygen carrier in the blood of many animals. The molecule consists of four subunits; in human adults, the subunits are two α-chains and two β-chains. Each subunit has a haem group embedded in it and approximately 150 amino-acid residues. The iron of the haem group, i.e. Fe-protoporphyrin-IX, is bound with a histidine residue in the polypeptide. The molecular weight of the haemoglobin is 64 500. Myoglobin, which is the oxygen-storage protein in muscle and other organs, in contrast, consists of a single chain that is very similar to the a- or β-chain of haemoglobin. The difference in the composition of the molecules makes a remarkable contrast in the oxygen-binding property of the two compounds. The curves of oxygen uptake versus oxygen pressure are shown in Figure VIII.18.1. The curve for myoglobin is a normal hyperbola whereas that for haemoglobin is sigmoidal.


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Copyright information

© Ei-Ichiro Ochiai and David R. Williams 1979

Authors and Affiliations

  • Ei-Ichiro Ochiai
    • 1
  • David R. Williams
    • 2
  1. 1.Department of ChemistryUniversity of British ColumbiaCanada
  2. 2.Department of ChemistryUniversity of Wales Institute of Science and TechnologyCardiffUK

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