人胰腺弹性蛋白酶的一种新型分离方法及一些特性

A novel method of isolation and some characteristic properties of human pancreatic elastases.

作者信息

Fujimoto K, Ogawa M, Saito N, Kosaki G, Minamiura N, Yamamoto T

出版信息

Biochim Biophys Acta. 1980 Mar 14;612(1):262-7. doi: 10.1016/0005-2744(80)90300-9.

Abstract

One component of elastases of human pancreatic juice and pancreatic extract was obtained in a highly purified state by chromatography on a column of sawdust. The elastase obtained after repeated adsorption chromatography with NaCl-containing buffers was almost homogeneous by gel filtration and polyacrylamide gel electrophoresis. This elastase showed relatively high elastolytic activity, but relatively low hydrolytic activity towards succinyl trialanine p-nitroanilide, as compared with another component of pancreatic juice elastase (which was not absorbed onto sawdust). Both elastases isolated were alkaline earth metal-dependent enzymes.

摘要

通过在木屑柱上进行色谱分离，从人胰液和胰腺提取物的弹性蛋白酶中获得了一种高度纯化的组分。用含氯化钠的缓冲液反复进行吸附色谱后得到的弹性蛋白酶，通过凝胶过滤和聚丙烯酰胺凝胶电泳显示几乎是均一的。与胰液弹性蛋白酶的另一种组分（未被木屑吸附）相比，这种弹性蛋白酶表现出相对较高的弹性溶解活性，但对琥珀酰 - 丙氨酰 - 对硝基苯胺的水解活性相对较低。分离得到的两种弹性蛋白酶都是依赖碱土金属的酶。