Abstract
InScylla serrata, haemolymph copper is bound to protein and it can be more reliably determined by the 2,2′ biquinoline method than by other spectrophotometric methods. Ionic or free copper is absent from the haemolymph. The lack of significant time-of-day variation in copper concentration and the occurrence of variation in total protein concentration and copper-protein ratio, indicate fluctuations in copper-free proteins, which may either be periodically sequestered or released by the tissues during different hours of the day.
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