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首页> 外文期刊>Current Science: A Fortnightly Journal of Research >Isolation of a serine Kunitz trypsin inhibitor from leaves of Terminalia arjuna
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Isolation of a serine Kunitz trypsin inhibitor from leaves of Terminalia arjuna

机译：从榄仁中提取丝氨酸Kunitz胰蛋白酶抑制剂

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摘要

A serine Kunitz protease inhibitor was isolated from the semi-mature leaves of Terminalia arjuna, a host plant for Antheraea mylitta, using ammonium sulphate fractionation, gel permeation chromatography and trypsin-sepharose affinity chromatography. A 29-fold purification of T. arjuna Trypsin Inhibitor (TaTI) with a yield recovery of 3.2% was achieved. The purified protease inhibitor (TaTI) was resolved into a single protein band corresponding to molecular weight of 19.0 kDa on 12% SDS-PAGE under non-reducing conditions, whereas an additional band of 21.5 kDa was observed when the same fraction was resolved on SDS-PAGE under reducing conditions in the presence of 2-mercaptoethanol. TaTI inhibited both trypsin and chymotrypsin, but showed higher affinity for trypsin compared to chymotrypsin. However, it is more effective on bovine trypsin than midgut trypsin of tasar silkworm. TaTI retains its activity over a wide range of temperatures (0-100 degrees C) and pH (2.0-8.0), with pH optimum of 8.0. These observations indicate that TaTI is not only specific to tasar silkworm but also to bovine serine proteases. Hence it can be considered as a generalist protease inhibitor.
机译：使用硫酸铵分级分离，凝胶渗透色谱法和胰蛋白酶-琼脂糖亲和色谱法从油葵花的寄主植物Terminalia arjuna的半成熟叶中分离出丝氨酸Kunitz蛋白酶抑制剂。达到了29倍的精制阿朱木霉胰蛋白酶抑制剂（TaTI）的回收率，回收率为3.2％。在非还原条件下，纯化的蛋白酶抑制剂（TaTI）在12％SDS-PAGE上解析为一条分子量为19.0 kDa的单一蛋白条带，而在SDS上分离相同级分时观察到了一条21.5 kDa的附加条带在2-巯基乙醇存在下在还原条件下进行-PAGE。 TaTI抑制胰蛋白酶和胰凝乳蛋白酶，但与胰凝乳蛋白酶相比对胰蛋白酶显示更高的亲和力。但是，它对牛胰蛋白酶比塔萨尔蚕的中肠胰蛋白酶更有效。 TaTI在很宽的温度范围（0-100摄氏度）和pH值（2.0-8.0）中保持其活性，最适pH值为8.0。这些观察结果表明，TaTI不仅对塔萨尔蚕具有特异性，而且对牛丝氨酸蛋白酶也具有特异性。因此，它可以被认为是一种通用蛋白酶抑制剂。

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