Berthillier G, Coleman R, Walker D G
Biochem J. 1976 Jan 15;154(1):193-201. doi: 10.1042/bj1540193.
A particulate glucokinase was recovered in the Golgi-rich fraction of rat liver prepared by the method of Morré [Methods Enzymol. (1971) 22, 130-148], thus extending the demonstration by Berthillier et al. [Biochim. Biophys. Acta (1973), 293, 370-378] of particulate glucokinase activity in a microsomal subfraction that showed enrichment in Golgi characteristics. The purity of this fraction was examined and it was then subjected to several treatments, the action of Triton X-100, freezing and thawing, and sonication to establish the topographical location of the glucokinase activity thus solubilized. The evidence suggests that the glucokinase activity is either soluble in the lumen of the Golgi apparatus or loosely associated with the inside of the Golgi membranes.
采用莫雷的方法[《酶学方法》(1971年)22卷,第130 - 148页]制备大鼠肝脏富含高尔基体的部分,从中回收了一种颗粒状葡萄糖激酶,从而扩展了贝蒂利耶等人[《生物化学与生物物理学报》(1973年),293卷,第370 - 378页]在显示高尔基体特征富集的微粒体亚组分中颗粒状葡萄糖激酶活性的证明。检查了该部分的纯度,然后对其进行了几种处理,即Triton X - 100的作用、冻融和超声处理,以确定如此溶解的葡萄糖激酶活性的拓扑位置。证据表明,葡萄糖激酶活性要么可溶于高尔基体腔,要么与高尔基体膜内部松散结合。