Yamamoto H, Tanaka M, Okochi T, Kishimoto S
Biochem Biophys Res Commun. 1983 Feb 28;111(1):36-40. doi: 10.1016/s0006-291x(83)80113-2.
Possible interactions of human liver and intestinal alkaline phosphatases with Cibacron Blue F3GA were examined. The results indicated that the intestinal enzyme bound to the dye column whereas the liver enzyme did not. The affinity of intestinal alkaline phosphatase with the dye-ligand appeared to be biospecific, since a low concentration of purine nucleoside phosphates or potassium phosphate specifically reversed the binding. Taking advantage of the variant alkaline phosphatase from human hepatocellular cancer tissue to behave on the dye adsorbent in a similar fashion with the intestinal enzyme, it was purified by Cibacron Blue F3GA affinity chromatography, producing a 189-fold purification with a yield of 93%.
研究了人肝脏和肠道碱性磷酸酶与汽巴克隆蓝F3GA之间可能的相互作用。结果表明,肠道酶与染料柱结合,而肝脏酶则不结合。肠道碱性磷酸酶与染料配体的亲和力似乎具有生物特异性,因为低浓度的嘌呤核苷磷酸或磷酸钾能特异性地逆转这种结合。利用人肝细胞癌组织中的变异碱性磷酸酶在染料吸附剂上的行为与肠道酶相似这一特点,通过汽巴克隆蓝F3GA亲和层析对其进行纯化,纯化倍数为189倍,产率为93%。