Isolation and blood coagulation inhibition of a new proteinase inhibitor from the sea anemone Anemonia sulcata

Abstract 1. 1. A new proteinase inhibitor was isolated from the sea anemone Anemonia sulcata and its inhibitory effect on the coagulation system investigated. The inhibitor was isolated by gel filtration, ion exchange chromatography and high pressure liquid chromatography. 2. 2. It is a strong basic polypeptide with a mol. wt of 6000–7000. 3. 3. The peptide inhibits the contact activation system and fibrinolysis. Results indicate that the peptide also inhibits the Russel's viper venom-induced factor X activation. 4. 4. Phylogenetically the inhibitor is the oldes member of the aprotinin-like family described so far.