Abstract
Hemocyanin of the Xiphosuran horseshoe crab, Limulus polyphemus, occurs as a 3.3 x 106 dalton protein (van Holde and van Bruggen, 19 71). The native multimer can be dissociated into a mixture of at least five subunit fractions whose functional properties differ from one another (Sullivan et al., 1974). The molecular weight of these subunits appears to be 66–70 x 103 and each appears to be an unique polypeptide (Bonaventura et al., 1975; Sullivan et al., 1976; Bonaventura et al., 1976).
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References
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Schutter, W.G., Van Bruggen, E.F.J., Bonaventura, J., Bonaventura, C., Sullivan, B. (1977). Structure, Dissociation and Reassembly of Limulus polyphemus Hemocyanin. In: Bannister, J.V. (eds) Structure and Function of Haemocyanin. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-66679-7_3
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DOI: https://doi.org/10.1007/978-3-642-66679-7_3
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