Kostareva I A, Orlievskaia O V, Iurchenko V S, Ponomareva R B, Samsonov G V
Prikl Biokhim Mikrobiol. 1981 May-Jun;17(3):430-5.
By chromatography on ultragel ACA-54 alpha-amylase was isolated from the enzymic preparation amylosubtilin G10x. As compared to the initial preparation, the specific activity of the purified enzyme per mg increased 25-fold. The major physico-chemical characteristics of alpha-amylase were determined. The molecular weight of the enzyme measured by gel-chromatography and electrophoresis was estimated to be 49,000. The isoelectric point determined by electrofocusing was found to be 5,2. Irreversible acid inactivation of the enzyme in the range of pH 2-5 was investigated. The reaction was found to develop in at least two stages.
通过在超凝胶 ACA - 54 上进行色谱分离，从淀粉酶制剂淀粉枯草杆菌蛋白酶 G10x 中分离出了α - 淀粉酶。与初始制剂相比，纯化后每毫克酶的比活性提高了 25 倍。测定了α - 淀粉酶的主要物理化学特性。通过凝胶色谱和电泳测得该酶的分子量估计为 49,000。通过等电聚焦测定的等电点为 5.2。研究了该酶在 pH 2 - 5 范围内的不可逆酸失活情况。发现该反应至少分两个阶段进行。
