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An Investigation of Haemocyanin Oxygen Affinity in the Semi-Terrestrial Crab Ocypode Saratan Forsk
Author(s) -
Stephen Morris,
C. R. Bridges
Publication year - 1985
Publication title -
journal of experimental biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.367
H-Index - 185
eISSN - 1477-9145
pISSN - 0022-0949
DOI - 10.1242/jeb.117.1.119
Subject(s) - hemolymph , bohr effect , hemocyanin , oxygen , biology , zoology , chemistry , biochemistry , oxygen–haemoglobin dissociation curve , genetics , organic chemistry , antigen
The oxygen affinity of the haemocyanin in the supralittoral crab Ocypode saratan was investigated at temperatures between 20 and 35 °C. The effect of L-lactate on dialysed and undialysed haemolymph oxygen affinity was also examined. In general, the temperature sensitivity of the haemocyanin was low: δH was −3.1kJ mol−1, between 25 and 30°C. Temperature sensitivity was temperature-dependent, being larger at the extreme temperatures (ΔH = −26kJ mol−1). The Bohr effect (ΔlogP50/ΔpH) was temperature-independent and averaged - 0.67. No specific effect of CO2 on oxygen affinity was observed but L-lactate increased oxygen affinity in both dialysed and undialysed haemolymph. The maximal effect of lactate on oxygen affinity was similar in dialysed and undialysed haemolymph, but was evident at a lower lactate concentration (4mmol1−1) in dialysed, compared with undialysed, haemolymph (7mmoll−1). Dialysed haemolymph showed a higher oxygen affinity than undialysed haemolymph at low lactate concentration (<4mmoll−1). The Bohr effect and buffer value both decreased with increasing lactate concentration in both dialysed and undialysed haemolymph. The physiological implications of these findings are discussed.

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