BUTYRATE KINASE FROM CLOSTRIDIUM ACETOBUTYLICUM

乙酰丁酸梭菌的一种丁酸激酶已纯化50倍 以31%的产率在五步法中实现均一。提纯 涉及硫酸铵分级，两种疏水相互作用 层析步骤、亲和层析和凝胶过滤。这个 等电点，天然和变性的分子量 酶、最适pH、底物专一性和氨基酸 测定了该酶的组成。丁酸盐抗体 目前，该蛋白正在一只兔子体内制备。这些将被用来 研究该酶的表达与发酵时间的关系。

A butyrate kinase from Clostridium acetobutylicum has been purified 50-fold to homogeneity in a five-step procedure with a 31% yield. The purification involved ammonium sulfate fractionation, two hydrophobic interaction chromatography steps, affinity chromatography, and gel filtration. The isoelectric point, the molecular weights of the native and denatured enzyme, the pH optimum, the substrate specificity, and the amino acid composition of the enzyme have been determined. Antibodies to butyrate kinase are currently being prepared in a rabbit. These will be used to study the expression of the enzyme as a function of fermentation time.