Buc J, Rivière M, Gontero B, Sauve P, Meunier J C, Ricard J
Eur J Biochem. 1984 Apr 2;140(1):199-202. doi: 10.1111/j.1432-1033.1984.tb08086.x.
A new method of purification of chloroplastic thioredoxins has been presented. This method is based on affinity chromatography on fructose-bisphosphatase--Sepharose columns. Two thioredoxin, fA and fB, may be extracted and purified to homogeneity from the same leaf extract. Whereas fA is monomeric and has an Mr of 11 400 +/- 500, fB is dimeric with an Mr of 18 000 +/- 600. The dimer dissociates in two halves in the ultracentrifuge under the effect of high pressures. Raising the ionic strength results in the same effect. Thioredoxins fA and fB activate to similar extents chloroplastic fructose bisphosphatase and NADP--malate dehydrogenase. Chloroplastic sedoheptulose bisphosphatase is activated by thioredoxin fB but not by thioredoxin fA.
已提出一种纯化叶绿体硫氧还蛋白的新方法。该方法基于在果糖二磷酸酶-琼脂糖柱上的亲和色谱法。两种硫氧还蛋白，fA和fB，可以从同一叶片提取物中提取并纯化至同质。fA是单体，Mr为11400±500，而fB是二聚体，Mr为18000±600。在高压作用下，二聚体在超速离心机中解离成两半。提高离子强度会产生相同的效果。硫氧还蛋白fA和fB对叶绿体果糖二磷酸酶和NADP-苹果酸脱氢酶的激活程度相似。叶绿体景天庚酮糖二磷酸酶被硫氧还蛋白fB激活，但不被硫氧还蛋白fA激活。
