一种通过巯基乙胺-Sepharose 亲和层析纯化菠菜叶光合果糖-1,6-二磷酸酶的新方法。
A new procedure for the purification of spinach leaf photosynthetic fructose-1,6-bisphosphatase by affinity chromatography on mercaptoethylamine-Sepharose.
机构信息
Unidad de Bioquímica Vegetal, Estación Experimental del Zaidín (C.S.I.C.), Granada, Spain.
出版信息
Photosynth Res. 1981 Dec;2(4):291-6. doi: 10.1007/BF00056266.
PMID:24470248
Abstract
A new purification procedure for spinach leaf fructose-1,6-bisphosphatase is proposed, which includes the use of affinity chromatography on mercaptoethylamine-Sepharose. A homogeneous preparation of the enzyme can be obtained in 48 hr, with a specific activity of 67 U/mg and a yield of 23%. The method may also be useful for the purification of other thioredoxin-activated chloroplast enzymes.
摘要
提出了一种新的纯化菠菜叶果糖-1,6-二磷酸酶的方法，该方法包括使用巯基乙胺-Sepharose 亲和层析。在 48 小时内可获得酶的均相制剂，比活性为 67 U/mg，收率为 23%。该方法也可能对其他硫氧还蛋白激活的叶绿体酶的纯化有用。
Zotero 插件