Letter | Published:

Spectral changes and allosteric transition in trout haemoglobin

Naturevolume 256pages761762 (1975) | Download Citation

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Abstract

PREVIOUS results have shown that two of the haemoglobin components from trout blood, Hb trout I and Hb trout IV, have different functional properties, which may be correlated directly with their physiological role (see ref. 1 for review). Thus, Hb trout I, which displays cooperative ligand binding at all pH values, completely lacks heterotropic interactions; on the other hand, these interactions are clearly evident in Hb trout IV, for which lowering of pH, or addition of organic phosphates, produces a large decrease in oxygen affinity and in cooperativity (n drops from 2.3 at pH 8 to 1 at pH 6)2,3.

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References

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    Brunori, M. in Current topics in cellular regulation, 9 (edit. by Horecker, B. L., and Stadman, E. R.), 1–39 (Academic, New York and London, 1975).

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    Binotti, I., et al., Archs Biochem. Biophys., 142, 274–280 (1971).

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    Brunori, M., et al., Eur. J. Biochem., 39, 563–570 (1973).

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    Brunori, M., Falcioni, G., and Rotilio, G., Proc. natn. Acad. Sci. U.S.A., 71, 2470–2472 (1974).

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    Barra, D., Bossa, F., Bonaventura, J., and Brunori, M., FEBS Lett., 35, 151–154 (1973).

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    Giardina, B., Brunori, M., Binotti, I., Giovenco, S., and Antonini, E., Eur. J. Biochem., 39, 571–579 (1973).

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    Perutz, M. F., Ladner, J. E., Simon, S. R., and Ho, C., Biochemistry, 13, 2163–2173 (1974).

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Affiliations

  1. Laboratory of Molecular Biology, University of Camerino, Camerino and CNR Centre of Molecular Biology, Institutes of Chemistry and Biochemistry, Faculty of Medicine, University of Rome, Rome, Italy

    • BRUNO GIARDINA
    • , FRANCA ASCOLI
    •  & MAURIZIO BRUNORI

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https://doi.org/10.1038/256761a0

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