ISOLATION AND ENZYMATIC CHARACTERISATION OF BRUSHBORDER-FRACTION OF RAT KIDNEY
ISOLATION AND ENZYMATIC CHARACTERISATION OF BRUSHBORDER-FRACTION OF RAT KIDNEY
复制标题
DOI：
10.1007/bf00588029
复制
发表时间：
1969-01-01
影响因子：
4.5
通讯作者：
KINNESAF.E
中科院分区：
文献类型：
--
作者：
KINNE, R;KINNESAF.E
刷边部分的分离是通过在等渗蔗糖介质中进行分式离心，然后在蔗糖密度梯度中进行分离来实现的。在密度d 1.16/d 1.17范围内。电镜观察显示球形碎片，微绒毛保存完好。碱性磷酸酶的比活性是整个匀浆的12倍。谷氨酸脱氢酶、乳酸脱氢酶和葡萄糖-6-磷酸酶活性降低。（Na++K+）刺激的、对瓦巴因敏感的atp磷酸水解酶被因子4富集，钾刺激的中性对硝基苯基磷酸酶表现出类似的行为。
The isolation of the brushborder-fraction is achieved by a fractional centrifugation in an isotonic sucrose medium followed by a separation in a sucrose density-gradient. The bruschborder-fragments sediment in the range of the density d 1.16/d 1.17. The electronmicroscopic investigation shows spherical fragments with well preserved microvilli. The specific activity of the alkaline phosphatase is twelve times higher than in the whole homogenat. The activity of the glutamate-dehydrogenase, lactate-dehydrogenase and the glucose-6-phosphatase is reduced. The (Na++K+)-stimulated, Ouabain sensitive ATP-phosphohydrolase is enriched by the factor four, the potassium-stimulated neutral p-nitrophenyl-phosphatase shows a similar behaviour.