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Hagfish Haemoglobins

  • Chapter
The Biology of Hagfishes

Summary

The properties of the haemoglobins of this phylogenetically ancient group of animals may shed light on evolution of haemoglobin (Hb) function in vertebrates. In contrast to the tetrameric haemoglobin molecules of other vertebrates, whose O2 affinity is modulated by organic phosphates found in the red blood cells, cyclostome Hbs are monomeric when oxygenated and exhibit no allosteric interaction with phosphates.

Hagfishes possess multiple haemoglobins, involving at least four components. The elec-trophoretic pattern of the haemoglobins varies significantly among individuals of the same species, reflecting polymorphism. The Hb components are essentially monomeric in the ligated (oxygenated) form. Some components aggregate to dimers and tetramers when deoxygenated. Aggregation is favoured by low pH and high protein concentration.

The Bohr effect (pH modulation of the oxygen affinity) in hagfish haemolysate is small and is due to the formation of (low-affinity) oligomers at low pH and (high-affinity) monomers at high pH. Oxygen binding is virtually non-cooperative, although the isolated tetrameric fraction of E. burgeri haemolysate shows haeme-haeme interaction. Bicarbonate ions (formed in the red blood cell by carbonic anhydrase-catalysed hydration of CO2) act as a potent allosteric effector in M. glutinosa haemolysate, causing a significant decrease in the oxygen affinity. This behaviour can be related to the virtual absence of the membrane protein Band III that is implicated in HCO3 -/C1- exchange. This anion-exchanger is similarly lacking in the red cell membranes of E. stoutii, suggesting that bicarbonate sensitivity may be a general character of hagfish haemoglobins.

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Authors
  1. Angela Fago
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  2. Roy E. Weber
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© 1998 Springer Science+Business Media Dordrecht

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Fago, A., Weber, R.E. (1998). Hagfish Haemoglobins. In: The Biology of Hagfishes. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5834-3_21

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  • DOI: https://doi.org/10.1007/978-94-011-5834-3_21

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-6465-1

  • Online ISBN: 978-94-011-5834-3

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