补骨脂胰蛋白酶抑制剂的亲和层析分离纯化和部分性质

Partly Characterization and Purification of Affinity Chromatography of Trypsin-inhibitor from Psoralea Corylifolia L.

本文介绍牛胰蛋白酶—对氨基苯砜乙基(ABSE)—Sepharose—4B的制备,及用此亲和吸附剂分离提纯补骨脂胰蛋白酶抑制剂的过程。用该方法对补骨脂胰蛋白酶抑制剂粗提物进行分离,可获得电泳单点纯样品。经SDS—PAGE电泳测定,该抑制剂的分子量为55000。等电聚焦电泳测定其等电点为pⅠ6.6,Chiff试剂染色为阴性。氨基酸组成分析結果表明含12种氨基酸,其中Gly、Glu含量最高。

This article describes the preparation of trypsin-ABSE-Sepharose-4B and the purification of affinity chromatography of trypsin-inhibitor from Psoralea Corylifolia L. The trypsin-inhibitor electrophoreses as a single band on PAGE and its molecular weight is measured on SDS-PAGE to be 55000 daltor. Its band with pI points of 6.6 on polyaerylamide IEF is not stained by Chiff's agent. It shows by amino acid composition analysis the presence of 12 classes of amino acids and there are more Gly and Glu among them.