Protease inhibitors from Ecballium elaterium seeds
- 1 March 1989
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 33 (3) , 202-208
- https://doi.org/10.1111/j.1399-3011.1989.tb00210.x
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 iso-inhibitors 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 .times. 1011 M-1) against trypsin, showing high Gly content, six half-cystine residues, but devoid of histidine, threonine, tryptophan, and tyrosine residues.Keywords
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