Joubert F J
Hoppe Seylers Z Physiol Chem. 1981 Nov;362(11):1515-21. doi: 10.1515/bchm2.1981.362.2.1515.
A proteinase inhibitor (DE-1) from the seed of Peltophorum africanum (Weeping wattle) was purified by chromatographic procedures involving Sephadex G-50, DEAE-cellulose and DEAE-Sepharose. It comprises 162 amino acid residues (molecular mass 18 000 Da) including 4 half-cystine residues and resembles the Kunitz-type proteinase inhibitors. The N-terminal primary structure of DE-1 showed homology with Kunitz soybean trypsin inhibitor and also with the proteinase inhibitors from Albizzia julibrissin and Erythrina latissima seeds. The inhibitor stoichiometrically inhibited trypsin and also alpha-chymotrypsin in the molar ratio of 1:1 and represents, therefore, a Kunitz-type double-headed proteinase inhibitor.
从非洲盾柱木（垂枝金合欢）种子中提取的一种蛋白酶抑制剂（DE-1），通过涉及葡聚糖凝胶G-50、二乙氨基乙基纤维素和二乙氨基乙基琼脂糖的色谱方法进行纯化。它由162个氨基酸残基组成（分子量18000道尔顿），包括4个半胱氨酸残基，与库尼茨型蛋白酶抑制剂相似。DE-1的N端一级结构与库尼茨大豆胰蛋白酶抑制剂以及合欢和刺桐种子中的蛋白酶抑制剂具有同源性。该抑制剂以化学计量比1:1抑制胰蛋白酶和α-糜蛋白酶，因此代表一种库尼茨型双头蛋白酶抑制剂。
