ISOLATION AND PURIFICATION OF CHLOROPLASTIC SPINACH (SPINACIA-OLERACEA) SEDOHEPTULOSE-1,7-BISPHOSPHATASE
ISOLATION AND PURIFICATION OF CHLOROPLASTIC SPINACH (SPINACIA-OLERACEA) SEDOHEPTULOSE-1,7-BISPHOSPHATASE
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DOI：
10.1042/bj2410071
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发表时间：
1987-01-01
影响因子：
4.1
通讯作者：
FERTE, N
中科院分区：
文献类型：
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作者：
CADET, F;MEUNIER, JC;FERTE, N
从菠菜叶绿体基质提取液中经DEAE-FractoGel、Sephadex G-200和Blue B亲和层析等步骤分离纯化了200多倍的高等植物七糖-1，7-二磷酸酯酶。它是一种M466,000的蛋白质，由两个明显相同的亚基组成(Mr 35,000)。在二硫苏糖醇存在的情况下，酶被还原的硫氧还蛋白FB激活。与1，6-二磷酸果糖相比，它对1，7-二磷酸七糖的特异性很高，但不是绝对的。
Higher-plant sedoheptulose-1,7-bisphosphatase was isolated and purified over 200-fold from spinach (Spinacia oleracea) chloroplast stromal extracts to apparent electrophoretic homogeneity by DEAE- Fractogel, molecular sieving on Sephadex G-200 and Blue B dye-matrix affinity chromatography. It is a protein of M4 66,000, made up of two apparently identical subunits (Mr 35,000). The enzyme is activated by reduced thioredoxin Fb in the presence of dithiothreitol. Its specificity towards sedoheptulose 1,7-bisphosphate versus fructose 1,6-bisphosphate is high, but not absolute.