Abstract
The oxygen-binding properties of Murex trunculus haemocyanin were described briefly by Wood and Dalgleish (1973) in a previous study from this laboratory. In the absence of divalent ions in the pH range 7.2–9.2, noncooperative oxygen binding and a small reverse Bohr effect were observed. In the presence of Mg2+, cooperative oxygen binding (with a Hill coefficient as large as 3 or more in some cases) and a more pronounced Bohr effect were seen. In a later study 50,000 molecular weight fragments (“Oxygen-binding domains”) of the haemocyanin, obtained by subtilisin digestion, were shown to bind oxygen noncoopera- tively, without a Bohr effect and with significantly decreased oxygen affinity with respect to untreated haemocyanin (Bannister et al., 1975). We describe here a systematic study of the oxygen equilibrium of Murex trunculus haemocyanin under various conditions of pH, divalent ion concentration and ionic strength. Oxygen-binding data are analysed in relation to cooperativity and linkage phenomena.
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References
Antonini, E., Brunori, M.: Hemoblobin and Myoglobin in Their Reactions with Ligands. Amsterdam: North Holland, 1971
Bannister, J.V., Galdes, A., Bannister, W.H.: Isolation and characterization of two- copper subunits from Murex trunoulus haemocyanin. Comp. Biochem. Physiol. 51B, 1–4 (1975)
Colosimo, A., Brunori, M., Wyman, J.: Concerted changes in an allosteric macromole- cule. In: Protein Ligand Interactions. Sund, H., Blauer, G. (eds.). Berlin: de Gruyter and Co., 1975, pp. 3–14
Er-el, Z., Shaklai, N., Daniel, E.: Oxygen-binding properties of haemocyanin from Levantina hierosolima. J. Mol. Biol. 64, 341–352 (1972)
Miller, K., Van Holde, K.E.: Oxygen binding by Callianassa califomiensis hemocyanin. Biochemistry 13, 1668–1674 (1974)
Salvato, B., Ghiretti-Magaldi, A., Ghiretti, F.: Acid-base titration of hemocyanin from Octopus vulgaris Lam. Biochemistry 13, 4778–4783 (1974)
Van Driel, R.: Oxygen binding and subunit interactions in Helix pomatia hemocyanin. Biochemistry 12, 2696–2698 (1973)
Van Driel, R., Van Bruggen, E.F.J.: Oxygen-linked association-dissociation of Helix pomatia hemocyanin. Biochemistry 13, 4079–4083 (1974)
Vannoppen-Ver Eecke, T., D’Hulster, R., Lontie, R.: Influence of the saturation with carbon monoxide and of deoxygenation on the alkaline dissociation of Helix pomatia haemocyanin. Comp. Biochem. Physiol. 46B, 499–507 (1973)
Vannoppen-Ver Eecke, T., Lontie, R.: The effect of alkaline earth ions on the co- operativity of the oxygenation of Helix pomatia haemocyanin. Comp. Biochem. Physiol. 45B, 945–954 (1973)
Williams, R.J.P.: The biochemistry of sodium, potassium, magnesium and calcium, Quart. Rev. 24, 331–365 (1970)
Wood, E.J., Dalgleish, D.G.: Murex trunulus haemocyanin. 2. The oxygenation reaction and circular dichroism. Europ. J. Biochem. 35, 421–427 (1973)
Wyman, J.: Linked functions and reciprocal effects in hemoglobin: a second look. Advan. Protein Chem. 19, 223–286 (1964)
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Bannister, J.V., Galdes, A., Bannister, W.H. (1977). The Oxygen Equilibrium of Murex trunculus Haemocyanin. In: Bannister, J.V. (eds) Structure and Function of Haemocyanin. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-66679-7_26
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DOI: https://doi.org/10.1007/978-3-642-66679-7_26
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-66681-0
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