Oxygen-binding properties of haemolymph from the benthic amphipod Monoporeia affinis from the Baltic

The Baltic benthic amphipod Monoporeia affinis (Lindström) has haemocyanin as a respiratory pigment. Haemocyanin constitutes ca. 90% of the total protein in the haemolymph. Oxygen affinity of the pigment is low, a P₅₀ of 4 kPa at pH?7.5 (6?°C). The Bohr factor (Δlog P₅₀/ΔpH) is also low, ?0.51, and the cooperativity coefficient, n₅₀, at P₅₀ is 1.5 to 2.5. The pigment characteristics point to a modest role of the haemocyanin, contrary to what could be expected for this sediment-living amphipod. It is suggested that physically dissolved oxygen is most important as oxygen supplier to the tissues.     

Anaerobic metabolism in the shrimp Crangon crangon exposed to hypoxia,anoxia and hydrogen sulfide

The brown shrimp Crangon crangon was collected in the Penzé estuary, Bretagne, in April 1994 and exposed to hypoxia, anoxia and combinations of hypoxia and sulfide. Exposure to sulfide induced total anaerobic metabolism even at an oxygen saturation which would otherwise permit totally aerobic metabolism. In addition to preventing aerobic metabolism there was a direct toxic effect of sulfide. Haemocyanin oxygen affinity (p₅₀) values from non-stressed C. crangon were relatively low. The p₅₀ values all exceed those where environmentally induced lactate accumulation occurs. It seems unlikely that lactate is an affinity modulating factor under environmental hypoxia.