Purification and some properties of two proteinase inhibitors (DE-1 and DE-3) from Erythrina latissima (broad-leaved erythrina) seed.
Two proteinase inhibitors, DE-1 and DE-3, were purified from Erythrina latissima seeds. Whereas DE-1 inhibits bovine chymotrypsin and not bovine trypsin, DE-3 inhibits trypsin but not chymotrypsin. The molecular weights and the amino acid compositions of the two inhibitors resemble the corresponding properties of the Kunitz-type proteinase inhibitors. The N-terminal primary structure of DE-3 showed homology with soybean trypsin inhibitor (Kunitz) and also with the proteinase inhibitors (A-II and B-II) from Albizzia julibrissin seed.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002241:Carbohydrates / Q000032:analysis; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D004895:Erythrina / Q000032:analysis*; D008970:Molecular Weight; D010940:Plant Proteins / Q000302:isolation & purification*; D010946:Plants, Medicinal; D011480:Protease Inhibitors / Q000302:isolation & purification*; D012639:Seeds / Q000032:analysis; D013045:Species Specificity; D014361:Trypsin Inhibitors / Q000302:isolation & purification
D000596:Amino Acids; D002241:Carbohydrates; D010940:Plant Proteins; D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; C031202:DE-3 protein, Erythrina latissima; D002918:Chymotrypsin