Burchell A, Burchell B, Monaco M, Walls H E, Arion W J
Biochem J. 1985 Sep 1;230(2):489-95. doi: 10.1042/bj2300489.
Hepatic microsomal glucose-6-phosphatase activity was rendered extremely unstable by a variety of techniques: (a) incubation at pH 5.0; (b) extraction of the microsomal fraction in the presence of 1% Lubrol; (c) various purification procedures. These techniques all result in the removal of a 21 kDa polypeptide from the fraction containing glucose-6-phosphatase activity. The 21 kDa protein was purified to apparent homogeneity by solubilization in the detergent Lubrol 12A-9 and chromatography on Fractogel TSK DEAE-650(S) and centrifugation at 105 000 g. The 21 kDa protein stabilizes glucose-6-phosphatase activity, whereas other purified hepatic microsomal proteins do not. The 21 kDa protein appears to be a potential regulator of glucose-6-phosphatase activity.
通过多种技术可使肝微粒体葡萄糖-6-磷酸酶活性变得极不稳定：(a) 在pH 5.0下孵育；(b) 在1% Lubrol存在的情况下提取微粒体部分；(c) 各种纯化程序。这些技术都会导致从含有葡萄糖-6-磷酸酶活性的部分中去除一种21 kDa的多肽。通过在去污剂Lubrol 12A-9中溶解、在Fractogel TSK DEAE-650(S)上进行色谱分离以及在105 000 g下离心，将该21 kDa蛋白质纯化至表观均一。该21 kDa蛋白质可稳定葡萄糖-6-磷酸酶活性，而其他纯化的肝微粒体蛋白质则不能。该21 kDa蛋白质似乎是葡萄糖-6-磷酸酶活性的潜在调节因子。
