Protease inhibitors from Ecballium elaterium seeds.
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.
Favel
A
A
INSERM U 58, Montpellier, France.
Mattras
H
H
Coletti-Previero
M A
MA
Zwilling
R
R
Robinson
E A
EA
Castro
B
B
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
D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D013381:Subtilisins; D002918:Chymotrypsin; D010196:Pancreatic Elastase