[大鼠红细胞6-磷酸葡萄糖酸脱氢酶电泳变体的纯化及某些性质]
[Purification and some properties of electrophoretic variants of 6-phosphogluconate dehydrogenase from rat erythrocytes].
作者信息
Serov O L, Manchenko G P, Khlebodarova T M
出版信息
Biokhimiia. 1975 Nov-Dec;40(6):1233-6.
Purification procedure of electrophoretic variants FF and SS of 6-phosphogluconate dehydrogenase (6-PGD) is described. The method includes (NH4)2SO4 fractionation and chromatography on DEAE- and CM-celluloses. Isoenzymes were purified about 5000 fold, and were found to be homogenous by disc electrophoresis in 7% polyacrylamide gel. It was found by comparative studies of activities of variants FF and SS, that pH optimum was 8.2 for variant FF and 8.8 for variant SS. Km for 6-phosphogluconate were found to be 17,5-10(-5) M for variants SS and FF respectively.
本文描述了6-磷酸葡萄糖酸脱氢酶（6-PGD）电泳变体FF和SS的纯化过程。该方法包括硫酸铵分级分离以及在DEAE-纤维素和CM-纤维素上进行色谱分离。同工酶被纯化了约5000倍，通过在7%聚丙烯酰胺凝胶中的圆盘电泳发现其为均一的。通过对变体FF和SS活性的比较研究发现，变体FF的最适pH为8.2，变体SS的最适pH为8.8。发现变体SS和FF对6-磷酸葡萄糖酸的Km分别为17.5×10⁻⁵M和10×10⁻⁵M。
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