Abstract
The structural and functional properties of hemocyanin from the mediterranean lobster Palinurus elephas have been recently published (1). The results obtained have shown that:
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a)
the protein exists in only two aggregation states (monomeric and hexameric);
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b)
the monomeric subunits are not homogeneous, but belong to at least 3 or 4 different classes; c) the 02 binding of the hexamer is cooperative, and both pH and (Ca++ dependent; d) the Bohr effect of the hexamer in the presence of Ca++ is negative and similar to that of the previously characterized Panulirus interruptus hemocyanin; e) the monomers are non cooperative and have relatively low 02 affinity (somewhat similar to that of the T state of the hexamer).
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References
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© 1986 Springer-Verlag Berlin Heidelberg
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Giardina, B. et al. (1986). Sexual and Seasonal Changes of Hc from Palinurus Elephas . In: Linzen, B. (eds) Invertebrate Oxygen Carriers. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71481-8_56
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DOI: https://doi.org/10.1007/978-3-642-71481-8_56
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-16943-7
Online ISBN: 978-3-642-71481-8
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