Purification and characterization of a trypsin inhibitor from rice bran.
Purification and characterization of a trypsin inhibitor from rice bran.
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米糠中胰蛋白酶抑制剂的纯化和表征。
DOI：
10.3177/jnsv.25.255
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发表时间：
1979
影响因子：
1.6
通讯作者：
Z. Maki
中科院分区：
文献类型：
--
作者：
M. Tashiro;Z. Maki
从米糠中分离纯化了一种胰蛋白酶抑制剂，经1%氯化钠提取、热处理、硫酸铵沉淀、CM-SephadexC-25离子交换层析和SephadexG-75凝胶过滤，得到一种胰蛋白酶抑制剂。通过电泳分析，最终制备物是均匀的。米糠胰蛋白酶抑制剂（RBTI）具有约14，500的分子量和8.07的等电点。氨基酸组成以碱性氨基酸、天冬氨酸、谷氨酸、脯氨酸和胱氨酸含量高为特点。BRTI抑制牛胰蛋白酶在1：1.6的底物-酶摩尔比。然而，它显示出对α-糜蛋白酶、胃蛋白酶、木瓜蛋白酶和枯草杆菌蛋白酶BPN '的抑制作用。
A trypsin inhibitor was isolated and purified from the bran of rice, Oryza sativa, by extraction with 1% sodium chloride, heat treatment, ammonium sulfate precipitation, ion-exchange chromatography on a CM-Sephadex C-25 and gel filtration on a Sephadex G-75. The final preparation was homogeneous by electrophoretic analysis. Rice bran trypsin inhibitor (RBTI) had a molecular weight of about 14,500 and an isoelectric point of 8.07. The amino acids, acid composition was characterized by high contents of basic amino acids, aspartic acid, glutamic acid, proline and cystine. BRTI inhibited bovine trypsin at an inhibitor-enzyme molar ratio of 1:1.6. It displayed, however, nobility to inhibit alpha-chymotrypsin, pepsin, papain and subtilisin BPN'.