Abstract
Abstract 1. 1. The single stripped, Hb of Lophius americanus (goosefish) has a P50 of approximately 1–2 mm Hg at neutral pH and exhibits cooperativity in oxygen binding. 2. 2. The hemoglobin exhibits a Bohr effect. The P50 is essentially independent of pH above 7.5, increases slightly between pH 7.5 and 7.0, and exhibits the largest increase between pH 7.0 and 6.5. 3. 3. ATP, and temperatures over 18°C decrease oxygen affinity. 4. 4. The P50 is essentially independent of chloride ion, hemoglobin concentration and temperatures below 18°C. No Root effect was observed. 5. 5. The amino acid composition of the two subunits indicates a minimum of six cysteines per tetramer with at least one on each alpha chain.
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