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通过连续亲和层析法分离九种人血浆蛋白酶抑制剂。

Isolation of nine human plasma proteinase inhibitors by sequential affinity chromatography.

作者信息

Dubin A, Potempa J, Travis J

机构信息

Institute of Molecular Biology, Jagiellonian University, Cracow, Poland.

出版信息

Prep Biochem. 1990;20(1):63-74. doi: 10.1080/00327489008050177.

Abstract

Purification of nine plasma proteinase inhibitors and one zymogen from a single batch of human plasma, using affinity chromatography has been accomplished. Those isolated were plasminogen (lysine-Sepharose), alpha-2-antiplasmin (plasminogen-Sepharose), high and low molecular weight kininogens (CM-papain-Sepharose), alpha-2-macroglobulin (Zn++ chelate-Sepharose), alpha-1-proteinase inhibitor, alpha-1-antichymotrypsin, Cl-inhibitor, inter-alpha-trypsin inhibitor (Blue-Sepharose) and antithrombin III (heparin-Sepharose). Alpha-2-macroglobulin and alpha-1-proteinase inhibitor required gel filtration as additional purification steps. Each protein was recovered in both high yield and purity.

摘要

已通过亲和层析从一批人血浆中纯化出九种血浆蛋白酶抑制剂和一种酶原。分离得到的有纤溶酶原(赖氨酸-琼脂糖凝胶)、α-2-抗纤溶酶(纤溶酶原-琼脂糖凝胶)、高分子量和低分子量激肽原(CM-木瓜蛋白酶-琼脂糖凝胶)、α-2-巨球蛋白(Zn++螯合琼脂糖凝胶)、α-1-蛋白酶抑制剂、α-1-抗糜蛋白酶、Cl-抑制剂、α-胰蛋白酶抑制剂(蓝色琼脂糖凝胶)和抗凝血酶III(肝素-琼脂糖凝胶)。α-2-巨球蛋白和α-1-蛋白酶抑制剂需要凝胶过滤作为额外的纯化步骤。每种蛋白质均以高产率和高纯度回收。

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