Bartlett D L, King C H, Poulter C D
Anal Biochem. 1985 Sep;149(2):507-15. doi: 10.1016/0003-2697(85)90606-2.
Farnesyl pyrophosphate synthetase (EC 2.5.1.1) from chicken liver, pig liver, and yeast has been purified to homogeneity in a single chromatographic step by affinity chromatography. The affinity ligand, geranylmethylphosphonophosphate, is linked to Affi-Gel 10 through the phosphonophosphate moiety. The affinity gel is stable chemically and the internal phosphonophosphate linkage is not hydrolyzed by nonspecific phosphatases. A single column has been used repeatedly for over a year with no degradation in its performance. A typical purification only requires 2 days and gives a 500- to 600-fold purification of enzyme from a crude ammonium sulfate precipitate.
通过亲和色谱法，已在单个色谱步骤中将来自鸡肝、猪肝和酵母的法尼基焦磷酸合酶（EC 2.5.1.1）纯化至同质。亲和配体香叶基甲基膦酸磷酸通过膦酸磷酸部分与Affi-Gel 10相连。亲和凝胶在化学上是稳定的，内部的膦酸磷酸键不会被非特异性磷酸酶水解。一根柱子已反复使用一年多，其性能没有下降。典型的纯化仅需2天，可使酶从粗硫酸铵沉淀中得到500至600倍的纯化。
