SATURATION OF HEMOGLOBIN WITH OXYGEN AT EQUILIBRIUM - Analytical Molecular Biology - page 63

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and enzymes exhibiting this behavior. Hemoglobin is just one of the
proteins which have been carefully analyzed. An enzyme, aspartate
transcarbamylase (Gerhart and Schachman, 1968), has also been extensively
studied.

To find other examples, the website <http://www.ncbi.nlm.nih.gov> can be
used to search for “allosteric enzymes” under PubMed. Several thousand
papers will be listed. However, careful measurements such as those of
Roughton et al. (1955) are rare. Without such experimental data, it would
be difficult to decide which models are more close to reality, as we have
clearly illustrated in this Chapter.

REFERENCES

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Arnone A (1972) X-ray diffraction study of binding of 2,3-diphosphoglycerate to human
deoxyhemoglobin. Nature, 237 , 146-149.

Battati S, Morrarelli A and Perutz MF (1998) Allosteric mechanism of hemoglobin: rupture
of salt-bridges raises the oxygen affinity of the T-structure. J. Mol. Biol., 281 , 581-585.

Eck RV and Dayhoff MO (1966) Atlas of Protein Sequence and Structure. National
Biomedical Research Foundation, Silver Springs, MD.

Edmundson AB (1965) Amino-acid sequence of sperm whale myoglobin. Nature, 205 , 883-
887.

Gerhart JC and Schachman HK (1968) Allosteric interactions in aspartate transcarbamylase.
II. Evidence for different conformational states of the protein in the presence and absence of
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Hill AV (1910) The possible effects of the aggregation of the molecules of hemoglobin on its
dissociation curves. J. Physiol., 40 , iv-vii.

Koshland DE Jr, Nemethy G and Filmer D (1966) Comparison of experimental binding data
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Monod J. Changeux J-P and Jacob F (1963) Allosteric proteins and cellular control systems.
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Monod J, Wyman J and Changeux J-P (1965) On the nature of allosteric transitions: a
plausible model. J. Mol. Biol, 12 , 88-118.

Nelson DL and Cox MM (2000) Lehninger Principles of Biochemistry, 3 rd Edition. Worth
Publishers, New York.