Saito A, Sinohara H
Department of Biochemistry, School of Medicine, Kinki University, Osaka-Sayama, Osaka, Japan.
Biol Chem. 1998 Nov;379(11):1367-70.
Alpha-1-antiproteinase E, the fourth isoform of rabbit alpha-1-antiproteinase (alpha-1-antitrypsin) having a glutamic acid at the reactive center, has been purified from the plasma by sequential chromatography on hydroxyapatite and anion-exchange columns. The E form of alpha-1-antiproteinase formed a complex with trypsin, chymotrypsin, elastase, plasmin and pancreatic kallikrein as judged by SDS-PAGE. The E form inhibited elastase in a stoichiometric manner and chymotrypsin moderately, but the inhibition of trypsin was gradual. The F form inhibited trypsin most effectively followed by chymotrypsin and elastase. N-chlorosuccinimide reduced the elastase inhibitory activity of the E form, while the F form was more effectively inactivated by the oxidant.
α-1-抗蛋白酶E是兔α-1-抗蛋白酶（α-1-抗胰蛋白酶）的第四种同工型，其反应中心含有谷氨酸，已通过在羟基磷灰石和阴离子交换柱上的连续色谱法从血浆中纯化出来。通过SDS-PAGE判断，α-1-抗蛋白酶的E型与胰蛋白酶、胰凝乳蛋白酶、弹性蛋白酶、纤溶酶和胰激肽释放酶形成复合物。E型以化学计量方式抑制弹性蛋白酶，对胰凝乳蛋白酶有中等程度的抑制作用，但对胰蛋白酶的抑制作用是渐进的。F型对胰蛋白酶的抑制作用最有效，其次是胰凝乳蛋白酶和弹性蛋白酶。N-氯代琥珀酰亚胺降低了E型的弹性蛋白酶抑制活性，而F型被氧化剂更有效地灭活。
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