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Functional properties of hemoglobins in the teleostTilapia grahami

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Summary

The oxygen binding properties ofTilapia grahami hemoglobins have been investigated. The whole blood hemolysate possesses at 35°C a high oxygen affinity (P 50∼ 4.0 mmHg). The O2Hb equilibrium is moderately affected by the ionic strenght chloride concentration) of the hemoglobin solution, while in contrast the temperature sensitivity of the O2Hb equilibrium was very high (ΔH=−20.0 kcal.mole−1).

Tilapia hemoglobin separated into 7 main fractions having nearly similar Bohr factors (−0.42<ø<−0.59) in a pH range from 7.2 to 7.6. The Bohr factor andn-value of the composite hemoglobins fell within the range for the individual Hb fractions. Addition of the organic nucleoside triphosphates, ATP and GTP, both occurring inTilapia grahami red cells, caused a marked increase inP 50 as well asn-values, with GTP having an effect nearly twice that of ATP on oxygen affinity.

Tilapia grahami lives in conditions of high alkalinity (9.6<pH<10.5), high temperature (T max≅43°C) and variable O2 concentration. The results are discussed in relation to hemoglobin function in this habitat.

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Authors and Affiliations

  1. Department of Zoophysiology, University of Aarhus, DK-8000, Aarhus, Denmark

    G. Lykkeboe &  K. Johansen

  2. Department of Animal Physiology, University of Nairobi, Nairobi, Kenya

    G. M. O. Maloiy

Authors
  1. G. Lykkeboe
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  2. K. Johansen
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  3. G. M. O. Maloiy
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Additional information

This work was supported by the Danish International Development Agency, the National Geographic Society and the Leverhulme Trust Funds.

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Lykkeboe, G., Johansen, K. & Maloiy, G.M.O. Functional properties of hemoglobins in the teleostTilapia grahami . J Comp Physiol B 104, 1–11 (1975). https://doi.org/10.1007/BF02482832

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  • DOI: https://doi.org/10.1007/BF02482832

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