绿色粘球菌胞外蛋白酶的纯化及特性
Purification and properties of an extracellular protease from Myxococcus virescens.
作者信息
Gnosspelius G
出版信息
J Bacteriol. 1978 Jan;133(1):17-25. doi: 10.1128/jb.133.1.17-25.1978.
Abstract
An extracellular protease from Myxococcus virescens was purified by phosphate precipitation, gel exclusion, and ion-exchange chromatography. The enzyme appeared homogeneous upon disc electrophoresis. The molecular weight of the protease was estimated to be 26,000. The enzyme was rapidly inactivated by ethylenediaminetetraacetate, but the activity could be partially restored by divalent cations. Diisopropylphosphorofluoridate inhibited enzyme activity completely. Michaelis-Menten kinetics were obeyed with casein and hemoglobin as substrates. First-order kinetics were obtained with elastin as the substrate, provided trypsin was in excess. Petidolytic activity indicated that the peptide bonds hydrolyzed by the enzyme were mainly those involving amino acids with nonpolar side chains.
摘要
通过磷酸盐沉淀、凝胶排阻和离子交换色谱法纯化了来自绿色粘球菌的一种细胞外蛋白酶。在圆盘电泳中该酶呈现均一性。该蛋白酶的分子量估计为26,000。该酶被乙二胺四乙酸迅速灭活，但二价阳离子可部分恢复其活性。二异丙基氟磷酸酯完全抑制酶活性。以酪蛋白和血红蛋白为底物时符合米氏动力学。以弹性蛋白为底物时，在胰蛋白酶过量的情况下获得一级动力学。肽水解活性表明该酶水解的肽键主要是那些涉及具有非极性侧链氨基酸的肽键。
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