Phosphoglucose isomerase from human erythrocyte. Preparation and properties.
Phosphoglucose isomerase from human erythrocyte. Preparation and properties.
复制标题
来自人红细胞的磷酸葡萄糖异构酶。
DOI：
--
复制
发表时间：
1971
期刊：
影响因子：
--
通讯作者：
C. H. Chervenka
中科院分区：
文献类型：
--
作者：
K. Tsuboi;K. Fukunaga;C. H. Chervenka
人红细胞磷酸葡萄糖异构酶（d-葡萄糖6-磷酸酮醇异构酶，EC 5.3.1.9）被分解为一个主要组分和两个次要组分。主要的酶形式，异构酶a，被纯化到恒定的比活性，并通过色谱，电泳和超离心分离呈现均一性。次要的酶形式，异构酶B和c，也以高纯度有限量制备。异构酶a、B和c的电荷性质略有不同（等电点分别为pH 9.2、9.1和9.0），但在分子大小的基础上无法区分。异构酶a的沉降速度和部分比容测量值为s20，w = 7.0 S和0.745 cm ~ 3/g。通过沉降平衡分析，天然酶的分子量为125，000，其中通过变性剂诱导解离产生两个相同或相似大小的亚基。异构酶a与B和c的区别在于果糖6-磷酸的Km较小。异构酶a、B和c与粗溶血产物在淀粉凝胶中电泳获得的主要和两种次要酶形式相同。
Abstract Phosphoglucose isomerase (d-glucose 6-phosphate ketol isomerase, EC 5.3.1.9) of the human erythrocyte was resolved into a major and two minor components. The major enzyme form, isomerase a, was purified to constant specific activity and appeared homogeneous by chromatography, electrophoresis, and ultracentrifugation. The minor enzyme forms, isomerases b and c, were also prepared in high purity in limited quantity. Isomerases a, b, and c differed slightly in their charge properties (isoelectric points at pH 9.2, 9.1, and 9.0, respectively) but were indistinguishable on the basis of molecular size. Sedimentation velocity and partial specific volume measure of isomerase a yielded values of s20, w = 7.0 S and 0.745 cm3 per g. Molecular weight of the native enzyme was 125,000 by sedimentation equilibrium analysis with dissociation induced by denaturing agents yielding two subunits of identical or similar size. Isomerase a was distinguishable from b and c on the basis of a lesser Km for fructose 6-phosphate. Isomerases a, b, and c were identifiable with the major and two minor enzyme forms obtained on electrophoresis of crude hemolysate in starch gel.