Joubert F J, Carlsson F H, Haylett T
Hoppe Seylers Z Physiol Chem. 1981 May;362(5):531-8. doi: 10.1515/bchm2.1981.362.1.531.
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.
从刺桐种子中纯化出两种蛋白酶抑制剂DE-1和DE-3。DE-1抑制牛胰凝乳蛋白酶而不抑制牛胰蛋白酶，而DE-3抑制胰蛋白酶但不抑制胰凝乳蛋白酶。这两种抑制剂的分子量和氨基酸组成与Kunitz型蛋白酶抑制剂的相应特性相似。DE-3的N端一级结构与大豆胰蛋白酶抑制剂（Kunitz）以及合欢种子中的蛋白酶抑制剂（A-II和B-II）具有同源性。
