Abstract
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.
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Received: 29 May 1997 / Accepted: 19 September 1997
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Hagerman, L., Sandberg, E. & Vismann, B. Oxygen-binding properties of haemolymph from the benthic amphipod Monoporeia affinis from the Baltic. Marine Biology 130, 209–212 (1997). https://doi.org/10.1007/s002270050240
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DOI: https://doi.org/10.1007/s002270050240