无机焦磷酸酶活性与人类碱性磷酸酶制剂的关联。
Association of inorganic-pyrophosphatase activity with human alkaline-phosphatase preparations.
作者信息
Moss D W, Eaton R H, Smith J K, Whitby L G
出版信息
Biochem J. 1967 Jan;102(1):53-7. doi: 10.1042/bj1020053.
Abstract
- The inorganic-pyrophosphatase activity of alkaline phosphatases prepared from human liver and small intestine was investigated at different stages of purification. 2. Both liver and intestinal preparations possessed pyrophosphatase activity at all stages of purification, and the two types of activity were not separated by gel filtration or by anion-exchange or cation-exchange chromatography. 3. After starch-gel electrophoresis of the tissue extracts, the zones of pyrophosphatase activity coincided exactly with alkaline-phosphatase zones. 4. Hydrolysis of each type of substrate was inhibited by the presence of the other, and a constant ratio of alkaline-phosphatase activity to pyrophosphatase activity was maintained during inactivation of the enzymes by incubation at 55 degrees . 5. These results are consistent with the view that alkaline phosphatases are also inorganic pyrophosphatases.
摘要
- 对从人肝脏和小肠制备的碱性磷酸酶在不同纯化阶段的无机焦磷酸酶活性进行了研究。2. 肝脏和小肠制剂在纯化的各个阶段均具有焦磷酸酶活性，且这两种活性不能通过凝胶过滤、阴离子交换或阳离子交换色谱法分离。3. 对组织提取物进行淀粉凝胶电泳后，焦磷酸酶活性区与碱性磷酸酶区完全重合。4. 一种底物的水解受到另一种底物存在的抑制，并且在55℃孵育使酶失活的过程中，碱性磷酸酶活性与焦磷酸酶活性保持恒定比例。5. 这些结果与碱性磷酸酶也是无机焦磷酸酶的观点一致。
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