Hauri H P, Green J R
Biochem J. 1978 Jul 15;174(1):61-66. doi: 10.1042/bj1740061.
Brush-border membranes were isolated from the rat small intestine and then treated with sodium dodecyl sulphate under non-reducing conditions at room temperature. Analysis of the solubilized components by polyacrylamide-gel electrophoresis identified three major glycoproteins that co-migrate with glucoamylase-maltase-sucrase, lactase and isomaltase-maltase-sucrase activities. High activities of alkaline phosphatase and trehalase were detectable, but they could not be attributed to distinct co-migrating protein bands. Analysis of mucosa from the distal small intestine by the same methods showed a pattern of bands different from that obtained with the proximal intestine, which appeared to correlate with the relative deficiency of some of the enzymes in the distal region.
从大鼠小肠中分离出刷状缘膜,然后在室温下非还原条件下用十二烷基硫酸钠处理。通过聚丙烯酰胺凝胶电泳对溶解成分进行分析,鉴定出三种主要糖蛋白,它们与葡糖淀粉酶 - 麦芽糖酶 - 蔗糖酶、乳糖酶以及异麦芽糖酶 - 麦芽糖酶 - 蔗糖酶活性共同迁移。可检测到碱性磷酸酶和海藻糖酶的高活性,但它们不能归因于明显共同迁移的蛋白条带。用相同方法对远端小肠黏膜进行分析,显示出的条带模式与近端小肠不同,这似乎与远端区域某些酶的相对缺乏相关。