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  • Title: Protease inhibitors from Ecballium elaterium seeds.
    Author: Favel A, Mattras H, Coletti-Previero MA, Zwilling R, Robinson EA, Castro B.
    Journal: Int J Pept Protein Res; 1989 Mar; 33(3):202-8. PubMed ID: 2654042.
    Abstract:
    Several protease inhibitors were found in the seeds of a Cucurbitacea, Ecballium elaterium, and were separated from one another by affinity and molecular sieve chromatography. Three main trypsin isoinhibitors were purified by ion-exchange chromatography and the sequence of the major one, EETI II, was elucidated and compared with other inhibitors of the squash family. It is a peptide of M.W. 3020 of strong inhibitory activity (Ka = 8 x 10(11) M-1) against trypsin, showing high Gly content, six half-cystine residues, but devoid of histidine, threonine, tryptophan, and tyrosine residues.
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