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Oxygen-binding properties of haemolymph from the benthic amphipod Monoporeia affinis from the Baltic
Hagerman, L.; Sandberg, E.; Vismann, B. (1997). Oxygen-binding properties of haemolymph from the benthic amphipod Monoporeia affinis from the Baltic. Mar. Biol. (Berl.) 130(2): 209-212
In: Marine Biology. Springer: Heidelberg; Berlin. ISSN 0025-3162; e-ISSN 1432-1793, meer
Peer reviewed article  

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Trefwoorden
    Biochemie; Eiwitten; Haemocyanins; Haemolymph; Mariene crustaceeën; Opgeloste zuurstof; Respiratory pigments; Zoöbenthos; Zuurstofverbruik; Monoporeia affinis (Lindström, 1855) [WoRMS]; Marien

Auteurs  Top 
  • Hagerman, L.
  • Sandberg, E.
  • Vismann, B.

Abstract
    The Baltic benthic amphipod Monoporeia affinis 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 ( Delta log P50 / Delta pH) 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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