title: Protease inhibitors from Ecballium elaterium seeds.
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.
authors.affiliation: INSERM U 58, Montpellier, France.
authors.forename: A
authors.initials: A
authors.lastname: Favel
authors.forename: H
authors.initials: H
authors.lastname: Mattras
authors.forename: M A
authors.initials: MA
authors.lastname: Coletti-Previero
authors.forename: R
authors.initials: R
authors.lastname: Zwilling
authors.forename: E A
authors.initials: EA
authors.lastname: Robinson
authors.forename: B
authors.initials: B
authors.lastname: Castro
mesh_terms: D000595:Amino Acid Sequence; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors; D011480:Protease Inhibitors / Q000302:isolation & purification*; D012639:Seeds / Q000032:analysis*; D013381:Subtilisins / Q000037:antagonists & inhibitors; D014361:Trypsin Inhibitors / Q000302:isolation & purification
chemical_list: D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D013381:Subtilisins; D002918:Chymotrypsin; D010196:Pancreatic Elastase