Abstract
Recently we have reported on the isolation of a mixture of trypsin isoinhibitors from snails (Helix pomatia) having broad inhibitory specificities [1-3]. The inhibitors were found to be secreted into the mucus of the snail [2]. Three homogeneous isoinhibitors B, E, and G have already been characterized [3]. We now have purified two other isoinhibitors H and K from the natural mixture I and wish to report on the amino acid sequence of the isoinhibitor K, the main component of the mixture.
Supported by the Deutsche Forschungsgemeinschaft.
Part of the Ph.-D. thesis, Technische Universität München 1974. Supported by the Founds der Chemischen Industrie.
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References
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Dietl, T., Tschesche, H. (1974). Amino Acid Sequence of Snail Inhibitor K and Correlation of Structure and Specificity. 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_30
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