碱性磷酸酶的研究。用32P标记的焦磷酸对小牛肠碱性磷酸酶进行磷酸化。
Studies on alkaline phosphatase. Phosphorylation of calf-intestinal alkaline phosphatase by 32P-labelled pyrophosphate.
作者信息
Fernley H N, Bisaz S
出版信息
Biochem J. 1968 Mar;107(2):279-83. doi: 10.1042/bj1070279.
Abstract
- A purified preparation of alkaline phosphatase from calf-intestinal mucosa was phosphorylated by (32)P-labelled PP(i) at a serine residue on the enzyme. Under the conditions employed, up to 0.15mum-labelled sites were obtained from 1mum-[(32)P]PP(i). 2. The phosphorylated enzyme was labile, the rate of dephosphorylation being similar to the overall rate of substrate hydrolysis. 3. A stopped-flow technique was used to determine the number of phosphomonoesterase active sites, which agreed with the number of (32)P-labelled sites. 4. It is concluded that calf-intestinal alkaline phosphatase is both a phosphomonoesterase and a pyrophosphatase.
摘要
- 从小肠黏膜提取的纯化碱性磷酸酶制剂，在酶的一个丝氨酸残基上被（32）P标记的焦磷酸（PPi）磷酸化。在所采用的条件下，从1μmol[（32）P]PPi中可获得高达0.15μmol标记位点。2. 磷酸化酶不稳定，去磷酸化速率与底物水解的总速率相似。3. 采用停流技术测定磷酸单酯酶活性位点的数量，其与（32）P标记位点的数量一致。4. 得出结论：小牛肠碱性磷酸酶既是磷酸单酯酶又是焦磷酸酶。
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