|On the variation in oxygen-binding properties in haemoglobins of lugworms (Arenicolidae, Polychaeta)|
Weber, R.E. (1972). On the variation in oxygen-binding properties in haemoglobins of lugworms (Arenicolidae, Polychaeta), in: Battaglia, B. (Ed.) Fifth European Marine Biology Symposium. pp. 231-243
In: Battaglia, B. (Ed.) (1972). Fifth European Marine Biology Symposium. Piccin Editore: Padova. 348 pp., more
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VLIZ: Proceedings 
|Document type: Conference paper|
The O sub(2) binding characteristics of Hbs from 3 species of Arenicolidae are measured and comparatively discussed with literature data. The Hbs appear of monophyletic origin. Since the molecular mechanism underlying the O sub(2) equilibria depend on the genetically determined primary protein structures, the functional characters were related to species differentiation. All Hbs have a high O sub(2) affinity, a diphasic oxygenation and strong haem-haem interactions. The pH influence on both O sub(2) affinity and haem-haem interaction, however, represents valid distinctions at the special level. The large variations of these intramolecular interactions in closely related species are concomitant with the views that the molecular adaptation results from the substitution of a small number of amino acid residues. The temperature sensitivity of O sub(2)-binding, like the O sub(2) affinity and the pH interaction, seems attributable to adaptive differentiation.