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  • 1995-1999  (2)
  • 1
    ISSN: 1573-5168
    Keywords: oxygen affinity ; Bohr effect ; temperature effect
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The aim of this study was to investigate the oxygen binding properties of the turbot (Scophthalmus maximus) hemoglobin polymorphism with special references to pH and temperature. Hemolysate samples from the three hemoglobin genotypes Hb- I(1/1), Hb-I(1/2) and Hb-I(2/2), were tested at 10, 16 and 19 °C and at pH values 7.2, 7.5 and 7.8 at 100 mm NaCl respectively. Hb-I(2/2) had the highest oxygen affinity at all three temperatures followed by Hb- I(1/2) and Hb-I(1/1). There was a significant decrease in oxygen affinity with increasing temperature and increasing pH in the range 10 to 19 °C for all three genotypes. The genotype Hb-I(1/1) had the highest Bohr effect followed by genotype Hb-I(2/2) and Hb-I(1/2). The effect was highest at 10 °C and decreased with temperature. Temperature sensitivity of the O2 binding for turbot hemoglobin was low and increased in general with increasing pH. It is hypothesised that the low sensitivity hemoglobins may be an adaptation to variable temperature conditions in the distribution area of the species.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 169 (1999), S. 329-334 
    ISSN: 1432-136X
    Keywords: Key words Haemoglobin ; Teleost fish ; Triplefins ; Oxygen transport ; Bohr effect
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Haemoglobin components were analysed for nine species of New Zealand triplefins and their isoelectric points (pI) ranged from 5.1 to 7.0. The number of well-expressed isohaemoglobins was larger in shallow-water and tidal pool species, ranging from four in Grahamina signata to eight in Grahamina capito, and were relatively cathodal. Two strongly anodal isohaemoglobins were expressed in the mid-depth species Ruanoho decemdigitatus and Ruanoho whero, and one in the deeper water species Karalepis stewarti and Forsterygion malcolmi. The red blood cell oxygen-binding properties were determined at 15 °C and 25 °C in the pH range 6.7–7.9 for the shallow-water species G. capito, the shallow to mid-depth species Forsterygion varium, and the deep-water species F. malcolmi. Oxygen affinity was highest for G. capito and the magnitude of the Bohr effect lower (Δlog P 50/ΔpH = −0.37 at 25 °C, where P 50 is the half-saturation coefficient) compared to the two Forsterygion species (Δlog P 50/ΔpH = −0.52 to −0.59). Further, the cooperativity factor, n 50, was lower in G. capito thus maintaining oxygen transport over a wide range of environmental oxygen pressures. Oxygen binding was similarly influenced by temperature in both G. capito and F. malcolmi (maximum heat of oxygenation ΔHmax = −27 kJ mol−1 and −37 kJ mol−1, respectively). Thus, triplefin fishes living in shallow, thermally unstable habitats possess a greater number of cathodally migrating isohaemoglobins, and their red blood cells have a higher oxygen affinity and reduced cooperativity which is less sensitive to changes in pH than do species occurring in more stable, deeper water habitats. Our analysis of an assemblage of closely related species circumvents some of the difficulties inherent in studies where interpretation of experimental results is confounded by phylogeny.
    Type of Medium: Electronic Resource
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