Abstract
Native 37S hemocyanin of the tarantula Eurypelma californicum shows a complex oxygen binding behavior with low oxygen affinity, strong normal Bohr effect, and high cooperativity (Hill coefficient beyond 7). All three effects are created by an interaction of the 24 constituent subunits, because isolated subunits have neither Bohr effect nor cooperativity, and their oxygen affinity is high (1). The oxygen binding behavior of the native 24-mer establishes itself by an interaction of two dodecamers which, on their part, consist of two interacting hexamers (2).
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© 1986 Springer-Verlag Berlin Heidelberg
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Markl, J. et al. (1986). Mercury Ions — A Tool to Study the Specific Role of Individual Subunits in the Allosteric Interaction of Arthropod Hemocyanins. In: Linzen, B. (eds) Invertebrate Oxygen Carriers. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71481-8_67
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DOI: https://doi.org/10.1007/978-3-642-71481-8_67
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