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Oxygen equilibria and ligand binding kinetics of erythrocruorins from two burrowing polychaetes of different modes of life, Marphysa sanguinea and Diopatra cuprea

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  • Roy E. Weber
  • J. Bonaventura, Duke University Marine Lab, USA
  • B. Sullivan, Duke University Marine Lab, USA
  • C. Bonaventura, Duke University Marine Lab, USA
Oxygen equilibria, ligand-binding kinetics and some other physicochemical properties are reported for erythrocruorins of two intertidal polychaetes:Marphysa sanguinea, which inhabits simple, relatively stagnant burrows, andDiopatra cuprea, which inhabits impermeable, parchment-like tubes that are vigorously ventilated.Marphysa erythrocruorin has a higher O2 affinity, which is less pH dependent (at pH 7.3 and 20øC, half-saturation O2 tension,P 50, and Bohr factor, =logP 50/pH, are 0.8 mm Hg and -0.25, respectively) than the corresponding parameters (P 50=5.5; =-0.86) inDiopatra (Figs. 1 and 2). In contrast to vertebrate haemoglobins, inorganic salts increase erythrocruorin O2 affinity (Fig. 3). The kinetic rates of ligand binding and dissociation ofMarphysa andDiopatra erythrocruorins (Tables 1 and 2) correlate well with the measured O2 affinities and appear to illustrate basic molecular adaptations of the two species to their respective micro-environmental conditions.
TidsskriftJournal of Comparative Physiology B: Biochemical, Systems, and Environmental Physiology
Sider (fra-til)177-184
Antal sider8
StatusUdgivet - 1978


  • roy, kinetics, erythrocruorin, invertebrates, ligands, annelid, hemoglobin, polychaetes, ligand binding, burrowing, oxygen equilibrium, Marphysa

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