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Oxygen-binding characteristics of three extra-cellular haemoglobins of Artemia salina
D'Hondt, J.; Moens, L.; Heip, J.; D'Hondt, A.; Kondo, M. (1978). Oxygen-binding characteristics of three extra-cellular haemoglobins of Artemia salina. Biochem. J. 171(3): 705-710
In: Biochemical journal. Biochemical Society: London. ISSN 0264-6021, more
Peer reviewed article  

Available in Authors 
    VLIZ: Open Repository 113287 [ OMA ]

Keywords
    Artemia salina (Linnaeus, 1758) [WoRMS]; Marine

Authors  Top 
  • D'Hondt, J.
  • Moens, L., more
  • Heip, J.
  • D'Hondt, A.
  • Kondo, M.

Abstract
    The oxygen-binding characteristics of the three extracellular haemoglobins of brine shrimp (Artemia salina) were studied in vitro by using highly purified preparations. Haemoglobin I is induced last in the development of brine shrimps when functional gills are formed. It has the lowest oxygen affinity (p50 5.34mmHg), an intermediate Bohr effect (ø -0.09 at 20°C) above pH8 and a temperature-sensitivity (DH -44.8 to -45.6kJ/mol at pH8–9) comparable with those observed with other invertebrate haemoglobins [Weber & Heidemann (1977) Comp. Biochem. Physiol. A 57, 151–155]. Haemoglobin II, which is the first to be induced, soon after hatching of nauplius larvae, persists generally throughout the whole adult life. It has an intermediate oxygen affinity (p50 3.7mmHg), the highest Bohr effect (ø -0.21 at 20°C) above pH8 and a similar temperature-sensitivity (DH -46.0 to -54.8kJ/mol at pH8–9) as haemoglobin I. However, haemoglobin III, which is induced second several hours after the induction of haemoglobin II but disappearing from the haemolymph in the middle of adult life, has the highest oxygen affinity (p50 1.8mmHg), the lowest Bohr effect (ø -0.03 at 20°C) above pH8.5 and a high resistance against temperature variation between 10 and 25°C at pH8.5–9 (DH -22.6 to -23.0kJ/mol). At pH7.5–8, haemoglobin III exhibits a similar temperature-sensitivity under 30°C as do other haemoglobins. All three haemoglobins have a rather low co-operativity, with Hill coefficients (h 1.6–1.9 at pH8.5), which are dependent on both pH and temperature. The highest co-operativity was observed at 20°C and pH9 for haemoglobins I and II, whereas it was at 27°C and pH8.5 for haemoglobin III. Thus the oxygen-binding behaviour of haemoglobin III in vitro is significantly different from those of haemoglobins I and II and indicates possibly its specific physiological role in vivo in the adaptive process in the natural environment.

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