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- W996074382 abstract "The sea anemone Anemonia sulcata contains abundant amounts of proteinase inhibitors. These are basic miniproteins of high stability that inhibit various serine proteinases such as trypsin, chymotrypsin, plasmin, plasma, and tissue kallikreins, and thus resemble aprotinin, the basic trypsin inhibitor from bovine organs. The inhibitory principle of A. sulcata can be separated by chromatography into at least 10 isoinhibitors that are similar in their amino acid compositions but differ in their abilities to inhibit kallikreins. This chapter describes the amino acid sequence of the main isoinhibitor 5 II in comparison with known inhibitory polypeptides of similar structure. Inhibitor 5 II from A. sulcata is homologous to the family of aprotinintype proteinase inhibitors. The inhibitor from the sea anemone shows a striking homology to the whole family, especially in regions that are invariant. From the results it is known that the amino acid residues with the most intimate contact to trypsin in the complex are in the regions glycine to arginine and glycine to arginine. The sequence homology of aprotinin and inhibitor 5 II from A. sulcata suggests a close similarity in the spatial arrangement of these two and other homologous polypeptides." @default.
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- W996074382 date "1981-01-01" @default.
- W996074382 modified "2023-10-14" @default.
- W996074382 title "[61] The broad-specificity proteinase inhibitor 5 II from the sea anemone Anemonia sulcata" @default.
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- W996074382 doi "https://doi.org/10.1016/s0076-6879(81)80063-8" @default.
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