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. 1966 Dec;101(3):852–860. doi: 10.1042/bj1010852

The properties and reactions of haemoglobin F1 and their bearing on the dissociation equilibrium of haemoglobin

E R Huehns 1,2, E M Shooter 1,2
PMCID: PMC1270194  PMID: 16742466

Abstract

1. Hb-FI, with the previously proposed structure αA2γFγAcF, would be an exception to the general hypothesis that haemoglobins are in mobile equilibrium with their sub-units at all pH values. However, studies presented in this paper suggest that this is not so. 2. Gel-filtration and sedimentation analyses show that Hb-FI dissociates at acid pH and gives only the usual types of hybrids in recombination experiments. When self-hybridized, Hb-FI is the main haemoglobin species re-formed, although small but increasing amounts of Hb-FII appear on prolonged exposure to acid. 3. Exchange experiments with isotopically labelled Hb-FII and unlabelled Hb-FI show no exchange of sub-units at neutral pH or after brief exposure to acid pH. Under equilibrium conditions at acid pH non-αA-chains do not exchange, although αA-chains equilibrate completely between the two species. 4. These results indicate that Hb-FI does not contain γF-chains and its possible structure is discussed on this basis. Since the dissociation properties of Hb-FI are not markedly different from those of Hb-A or Hb-FII it is concluded that Hb-FI, like other haemoglobins, is an equilibrium system.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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