Serine- and SH-proteinase inhibitors from Enterolobium contortisiliquum beans. Purification and preliminary characterization.
Two types of proteinase inhibitors were purified from Enterolobium contortisiliquum beans. The inhibitor of serine-proteinases inhibited trypsin (Ki = 5 nM), chymotrypsin (Ki = 10 nM) and plasma kallikrein, but not tissue kallikreins. The molecular weight is approximately 23 kDal and two polypeptide chains are detected after reduction. The second inhibitor with activity directed against SH-proteinases was isolated by CM-papain-Sepharose. The molecular weight is approximately 60 kDal and only one polypeptide chain was detected after reduction. Papain (Ki = 0.6 nM) and bromelain are inhibited.
D015853:Cysteine Proteinase Inhibitors / Q000302:isolation & purification; D007887:Fabaceae; D010946:Plants, Medicinal; D011480:Protease Inhibitors / Q000302:isolation & purification*; D012697:Serine Endopeptidases; D015842:Serine Proteinase Inhibitors / Q000302:isolation & purification
D015853:Cysteine Proteinase Inhibitors; D011480:Protease Inhibitors; D015842:Serine Proteinase Inhibitors; D012697:Serine Endopeptidases