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Laboratory Experiments

Experiment 18 Haemoglobin — Oxygenation, and Magnetic and Spectroscopic Studies

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Laboratory Introduction to Bio-inorganic Chemistry

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Abstract

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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Author information

Authors and Affiliations

  1. Department of Chemistry, University of British Columbia, Canada

    Ei-Ichiro Ochiai BSc, PhD

  2. Department of Chemistry, University of Wales Institute of Science and Technology, Cardiff, UK

    David R. Williams BSc, PhD, CChem, FRIC, DSc

Authors
  1. Ei-Ichiro Ochiai BSc, PhD
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  2. David R. Williams BSc, PhD, CChem, FRIC, DSc
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© 1979 Ei-Ichiro Ochiai and David R. Williams

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Ochiai, EI., Williams, D.R. (1979). Laboratory Experiments. In: Laboratory Introduction to Bio-inorganic Chemistry. Palgrave, London. https://doi.org/10.1007/978-1-349-86127-9_8

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