Abstract
1. 1. The most pronounced sigmoidal oxygenation curve is obtained for Helix pomatia haemocyanin, in the absence of buffer, at pH 7·9 in the presence of 6 mM Ca 2+ or 10 mM Sr 2+. Mg 2+ and Ba 2+, on the contrary, have no effect on the co-operativity of the oxygenation. 2. 2. The influence of alkaline earth ions on the stabilization of H. pomatia haemocyanin at pH 7·9 follows a different order: Ca 2+>Mg 2+>Sr 2+ = Ba 2+, suggesting two types of binding sites. The type with the higher affinity could be responsible for the stabilization, the type with the lower affinity for the co-operativity of the oxygen binding. 3. 3. An interpretation is suggested for the co-operative oxygen binding of H. pomatia haemocyanin by postulating a deoxy and an oxy structure in a relaxed and in a tense state. In the relaxed state the transition between the two structures is easy and the oxygen affinity high, in the tense state, stabilized at pH 7·9 by Ca 2+ or Sr 2+, the transition is difficult and the oxygen affinity low.
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More From: Comparative Biochemistry and Physiology -- Part B: Biochemistry and Molecular Biology
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