Scopes R K
Anal Biochem. 1984 Feb;136(2):525-9. doi: 10.1016/0003-2697(84)90256-2.
2-Keto-3-deoxy-6-phosphogluconate aldolase (EC 4.1.2.14) has been isolated from extracts of Zymomonas mobilis using differential dye-ligand chromatography and affinity elution with product/product analog. The one-step procedure gives an enzyme with specific activity 600 units mg-1. Only 1 out of 47 dyes, Procion Yellow MX-GR, bound the enzyme completely in 20 mM phosphate buffer, pH 6.5. A column of Navy HE-R adsorbent was used first to remove most of the potentially adsorbing proteins.
利用差异染料配体色谱法和产物/产物类似物亲和洗脱,从运动发酵单胞菌提取物中分离出了2-酮-3-脱氧-6-磷酸葡萄糖酸醛缩酶(EC 4.1.2.14)。该一步法得到的酶比活性为600单位mg-1。在47种染料中,只有普施安黄MX-GR这一种染料能在pH 6.5的20 mM磷酸盐缓冲液中完全结合该酶。首先使用海军HE-R吸附剂柱去除大部分潜在的吸附性蛋白质。