Purification and some properties of two proteinase inhibitors from Erythrina acanthocarpa seed.
Two proteinase inhibitors (DE-1 and DE-2) were purified from Erythrina acanthocarpa seed by gel filtration followed by ion exchange chromatography on DEAE-cellulose and DEAE-sepharose. They contain 163-164 amino acids (molecular weight 18000) including four half-cystine residues and resemble the Kunitz-type proteinase inhibitors. The N-terminal amino acid sequence of DE-1 also shows homology with those of the Kunitz-type inhibitors. For DE-2 no free N-terminal amino acid was found. DE-1 contains a potent inhibitor for both porcine trypsin and bovine alpha-chymotrypsin. Inhibitor DE-2 inhibits alpha-chymotrypsin strongly and it has practically no action on trypsin.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004589:Electrophoresis, Disc; D004895:Erythrina / Q000032:analysis*; D008970:Molecular Weight; D010946:Plants, Medicinal; D011480:Protease Inhibitors / Q000302:isolation & purification* / Q000494:pharmacology; D012639:Seeds / Q000032:analysis
D000596:Amino Acids; D011480:Protease Inhibitors