Purification of an Aspergillus oryzae Metallo-proteinase by Talopeptin-aminohexyl-Sepharose and Its Properties
1984 年 48 巻 6 号 p. 1533-1538
詳細
1984 年 48 巻 6 号 p. 1533-1538
Simple and speedy purification of Aspergillus oryzae metallo-proteinase was performed using Talopeptin-aminohexyl-Sepharose. The properties of the metallo-proteinase were: optimum pH 6.5; pH stability, pH 5-11; optimum temperature, 50°C; and molecular weight 42, 000 (SDS electrophoresis). These results were similar to those of neutral protease I from Aspergillus oryzae reported by Nakadai et al. This metallo-proteinase was compared with others from microbes using the metallo-proteinase inhibitors FMPI, PLT, and Talopeptin. The metallo-proteinase is unique in the point at which FMPI and PLT gave nearly stoichiometrical inhibition.
この記事は最新の被引用情報を取得できません。
