n African Entomology - The effect of temperature on the pH, d-lactate and haemocyanin oxygen affinity of (Koch) (Scorpionidae) haemolymph : research article

Volume 18, Issue 1
  • ISSN : 1021-3589



The pH and d-lactate of the haemolymph from the scorpion, , were measured at different ambient temperatures. The oxygen affinity and molecular cooperativities of haemocyanin in its native and dialysed form were determined when exposed to different ambient temperatures. D-lactate concentration in native haemolymph increased significantly from 0.31 mmol/l at 7°C to 1.93 mmol/l when haemolymph was exposed to 25°C for 6 hours but decreases to 0.32 mmol/l at 37°C. The extinction coefficients of haemocyanin at 240 nm and 278 nm were 2.41 and 11.26, respectively, and correspond well with similar data on the crustacean . The subunit cooperativity () of the native haemocyanin molecule increased linearly from = 3.00 to = 5.34 at 37°C. A d-lactate effect on between pH 7.40 and 7.87 could be demonstrated while the heat of oxygenation (∆) was -127.64 kJ/mol between 17°C and 25°C. Like other scorpions investigated, haemocyanin of exposed to wide temperature regimes show a strong temperature dependence of oxygen affinity (as ) and cooperativity (as ).

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