刺蒴麻种子中两种蛋白酶抑制剂的纯化及某些性质
Purification and some properties of two proteinase inhibitors from Erythrina acanthocarpa seed.
作者信息
Joubert F J
出版信息
J Nat Prod. 1982 Jul-Aug;45(4):427-33. doi: 10.1021/np50022a011.
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.
从具刺刺桐种子中通过凝胶过滤，随后在DEAE - 纤维素和DEAE - 琼脂糖上进行离子交换色谱法纯化出两种蛋白酶抑制剂（DE - 1和DE - 2）。它们含有163 - 164个氨基酸（分子量18000），包括四个半胱氨酸残基，类似于Kunitz型蛋白酶抑制剂。DE - 1的N末端氨基酸序列也显示出与Kunitz型抑制剂的同源性。对于DE - 2，未发现游离的N末端氨基酸。DE - 1对猪胰蛋白酶和牛α - 胰凝乳蛋白酶均有强效抑制作用。抑制剂DE - 2对α - 胰凝乳蛋白酶有强烈抑制作用，而对胰蛋白酶几乎没有作用。
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