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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Algebra universalis 1 (1960), S. 451-511 
    ISSN: 1420-8911
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 115 (1977), S. 171-184 
    ISSN: 1432-136X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The subunit structure, association equilibria, and oxygen binding of the hemocyanins of three thalassinid shrimp have been investigated. The organismsCallianassa californiensis, Callianassa gigas andUpogebia pugettensis are found in similar but distinct habitats in a limited region. All of the hemocyanins exhibit a common pattern of subunit structure, but differ in details of the response of that structure to variations in ionic environment. All three are heterogeneous in polypeptide chain composition, but have quite different distributions of components. The oxygen binding of the twoCallianassa hemocyanins is virtually identical under conditions approximating physiological; that ofUpogebia, which shows lower tolerance to anoxia, is significantly different. These similarities and differences are discussed in terms of the physiological requirements of the species.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 143 (1981), S. 253-260 
    ISSN: 1432-136X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Callianassa californiensis has two hemocyanins present in the blood, a 39 S form and a 17 S form. It does not regulate major blood ions with decreasing salinity, thus the ion levels can drop dramatically in winter when estuarine seawater becomes more dilute. Its hemocyanin shows remarkably little functional change when salinity is reduced from 35‰ to 17.5‰. At normal blood pH (∼ 8.2 at 10°C) the affinity decreases from 2.5 to 4.5 mm Hg with lowered salinity. The Bohr effect curves at both salinities have a complex biphasic shape with an average slope of −1.59, but they differ in affinity so they are parallel through the pH range 7.0 to 9.0. Cooperativity remains the same at every pH for the two Bohr series with maximumn H≅3.5 at physiological pH. There is no change in blood pH at low salinity. The 39 S and 17 S hemocyanins have similar affinities but the cooperative behavior is different. Adding NaCl and KCl to physiological levels slightly decreases affinity compared to MgCl2 and CaCl2 alone. Lowering temperature increases affinity.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 143 (1981), S. 261-267 
    ISSN: 1432-136X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Callianassa, an estuarine animal, can experience changes in salinity which reduce the level of divalent cations in the blood, as well as changes in temperature and variations in protein concentration in the hemolymph. The hemocyanin in whole hemolymph shows evidence of dissociation (∼ 12%) after 3 days acclimation to 40% seawater. Using purified hemocyanin the dissociation from 39 S to 17 S hemocyanin was investigated for the three variables, salinity, temperature and protein concentration. An equation was developed to define the amount of dissociation which should be observed under physiological conditions.
    Type of Medium: Electronic Resource
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