Abstract
The haemocyanin of the Roman snail (Helix pomatia) consists of an α- (75%) and a β-component (25%), both having a molecular weight of 9 × 106 (Wood et al., 1971) and a copper content of the order of 0.25% (2 Cu/ 50,000 on the average). The α-component dissociates into halves in the presence of 1 M NaCl or KC1 (Heirwegh et al., 1961) or in slightly alkaline medium, pH 7.0–7.6 (Witters and Lontie, 1968), while the β- component does not. At higher pH values both haemocyanins successively dissociate into tenths and twentieths (Witters and Lontie, 1968; Siezen and van Driel, 1974). As the twentieths do not dissociate further under mild conditions, they most probably correspond to the polypeptide chains of the haemocyanin molecule.
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Gielens, C., Preaux, G., Lontie, R. (1977). Structural Investigations on β-Haemocyanin of Helix pomatia by Limited Proteolysis. 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_11
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DOI: https://doi.org/10.1007/978-3-642-66679-7_11
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