Abstract
1. 1. Dissociation of lobster hemocyanin was broguht about by changes in pH. The effect of dissociation and reassociation of subunits on the oxygen equilibrium characteristics of hemocyanin was studied. Dissociation was determioned by ultracentrifugation and electrophoresis. Oxygen dissociation curves were obtained using a tonometer equipped with both a polarographic sensor and a 1 -cm quartz cuvette. 2. 2. The hemocyanin molecule remained aggregated between pH 4·5 and pH 8·5. Subuniting occured between both pH 3·0–4·5 and pH 8·5–10·5. The subunits sedimented with values of 8·5 S and 6·5 S, while the aggretated form of the molecule and an average value of 16·0 S. 3. 4. The reassociation of subunits was not complete, and although the autocatalytic nature of the ligand-binding reaction was not chagned in reassociated hemocyanin, the total amount of oxygen bound per molecule was slightly less. 4. 5. The numner of ligand-binding sites per molecule, as indicated by Hill equation analysis, is at least four.
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