Abstract
Digestion of whole native molecules of Lymnaea stagnalis haemocyanin with trypsin resulted in the formation of “tubes” of digested haemocyanin molecules, some 20 to 30 times the length of the original molecule. Removal of the tubes by preparative ultracentrifugation left in the supernatant a fragment of tryptic digestion which bound oxygen. This fragment had a slightly different absorption spectrum to both native haemocyanin and to tubes. It appeared to be homogeneous in size with a molecular weight of approximately 124,000 and a polypeptide chain weight of approximately 45,000. The material was however heterogeneous in charge.
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© 1977 Springer-Verlag Berlin Heidelberg
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Wood, E.J. (1977). Digestion of Lymnaea stagnalis Haemocyanin with Trypsin. 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_10
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DOI: https://doi.org/10.1007/978-3-642-66679-7_10
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-66681-0
Online ISBN: 978-3-642-66679-7
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