Abstract
Molluscan hemocyanins appear to be composed of polypeptide subunits of unusually large size. It is known that these large subunits can be fragmented without denaturation by treatment with the proteolytic enzyme subtilisin. Some of the chromatographic zones are homogeneous, as evidenced by single bands in regular and SDS-gel electrophoresis. These artificial subunits or domains have molecular weights in the range of 50,000. Functional heterogeneity of these artificial subunits is indicated by differences in their oxygen affinities and in their pH and NaCl sensitivities. In contrast, subtilisin digestion of an arthropodan hemocyanin, that of Limulus polyphemus, cleaves peptide bonds, but fragments are not observed unless the molecule is denatured.
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References
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Bonaventura, J., Bonaventura, C., Sullivan, B. (1977). Properties of the Oxygen-Binding Domains Isolated from Subtilisin Digests of Six Molluscan Hemocyanins. 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_27
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DOI: https://doi.org/10.1007/978-3-642-66679-7_27
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