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[作为用于分离白细胞弹性蛋白酶的亲和配体的鲍曼-伯克大豆抑制剂。对白细胞弹性蛋白酶催化的弹性蛋白水解的抑制作用]

[Bowman-Birk soy inhibitor as an affinity ligand for isolating leukocyte elastase. Inhibition of elastin hydrolysis, catalyzed by leukocyte elastase].

作者信息

Tikhonova T V, Larionova N I, Gladysheva I P, Kazanskaia N F

出版信息

Biokhimiia. 1993 Nov;58(11):1669-76.

PMID:8268308
Abstract

A one-step procedure for human leukocyte elastase purification using an affinity adsorbent based on protein soybean Bowman-Birk proteinase inhibitor has been developed. The leukocyte elastase was purified 70-fold with a 70-100% yield. The enzyme preparations did not contain cathepsin G and displayed a high specific activity. The soybean Bowman-Birk type inhibitor effectively inhibited the elastin hydrolysis by leukocyte elastase both when the enzyme and the inhibitor were simultaneously added to the substrate and after preliminary elastase adsorption on elastin. The inhibitory effect was preserved at high degrees of elastin hydrolysis.

摘要

已经开发出一种基于大豆Bowman-Birk蛋白酶抑制剂的亲和吸附剂一步法纯化人白细胞弹性蛋白酶的方法。白细胞弹性蛋白酶的纯化倍数为70倍,产率为70%-100%。酶制剂不含组织蛋白酶G,且具有较高的比活性。当酶和抑制剂同时添加到底物中以及弹性蛋白酶预先吸附在弹性蛋白上之后,大豆Bowman-Birk型抑制剂均能有效抑制白细胞弹性蛋白酶对弹性蛋白的水解作用。在高度弹性蛋白水解的情况下,抑制作用依然存在。

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