Abstract
The high content of proteinase inhibitors present in snails (Helix pomatia) [1] (this volume, p. 254) stimulated similar investigations on another species of the mollusca. Cuttle fish (Loligo vulgaris) contains a complex mixture of inhibitors [2] which could be resolved by gradient equilibrium chromatography [3] on SE-Sephadex C-25 (Fig. 1). Four inhibitors A, B, E, and L were separated and three of them were purified to homogeneity, namely isoinhibitors A, B, and E. This new class of inhibitors is characterized by a total number of 62 amino acid residues containing 4 disulfide bridges. On the basis of their amino acid composition all are isoinhibitors which only differ by a certain number of amino acid substitutions (Table 1), but significant differences have been found in their inhibitory specificities.
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References
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Tschesche, H., Von Rücker, A. (1974). Discussion Remark. In: Fritz, H., Tschesche, H., Greene, L.J., Truscheit, E. (eds) Proteinase Inhibitors. Bayer-Symposium, vol 5. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-87966-1_34
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DOI: https://doi.org/10.1007/978-3-642-87966-1_34
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