The binding of alkaline earth ions by the haemocyanin of Helix pomatia L.

Burton, R.F. (1972) The binding of alkaline earth ions by the haemocyanin of Helix pomatia L. Comparative Biochemistry and Physiology Part A: Physiology, 41(3), pp. 555-565. (doi: 10.1016/0300-9629(72)90013-8)

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1. Within physiological limits of pH and ionic concentrations, the amount of calcium bound by haemocyanin (m-mole/g) is approximately equal to F[Ca0]/([Ca0]+0·65 [Mg0]+K), where square brackets denote millimolal concentrations of free ion, F = 0·73(pH−4)−0·0433(pH)2 and K = 4·70(9·445−pH). 2. The affinity of magnesium for haemocyanin at a given pH is 0·65 times that of calcium, while the affinities of both strontium and barium for haemocyanin are about half that of calcium. 3. Significant amounts of calcium and magnesium are bound by haemocyanin in the haemolymph of Helix pomatia, but the equilibria of calcium, magnesium and hydrogen ions with haemocyanin do not seem important in ionic regulation. 4. Haemocyanin from H. aspersa binds calcium at pH 8 to about the same extent as does haemocyanin from H. pomatia.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Burton, Dr Richard
Authors: Burton, R.F.
College/School:College of Medical Veterinary and Life Sciences > School of Life Sciences
Journal Name:Comparative Biochemistry and Physiology Part A: Physiology
Publisher:Pergamon Press

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