Phosphorylcholine as a unique substrate for human intestinal alkaline phosphatase |
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| Affiliation: | 2. First Department of Biochemistry, Saitama Medical School, 38 Morohongo Moroyama, Iruma-gun, Saitama 350-04, Japan;1. Department of Endocrinology, The First Affiliated Hospital of Dalian Medical University, 222 Zhongshan Road, Xigang District, Dalian 116011, China;2. Department of Nutrition, The First Affiliated Hospital of Dalian Medical University, 222 Zhongshan Road, Xigang District, Dalian 116011, China;3. Dalian Key Laboratory of Prevention and Treatment of Metabolic Diseases and the Vascular Complications, 222 Zhongshan Road, Xigang District, Dalian 116011, China;1. Beijing Key Laboratory of Materials Utilization of Nonmetallic Minerals and Solid Wastes, National Laboratory of Mineral Materials, School of Materials Science and Technology, China University of Geosciences, Beijing 100083, PR China;2. Key Laboratory of Chemical Sensing&Analysis in Universities of Shandong, School of Chemistry and Chemical Engineering, University of Jinan, Jinan 250022, PR China;1. School of Chemistry and Materials Science, Ludong University, 264025 Yantai, Shandong Province, People’s Republic of China;2. School of Information and Electronic Engineering, Shandong Technology and Business University, 264005 Yantai, Shandong Province, People’s Republic of China;1. State Key Laboratory of Analytical Chemistry for Life Science and Collaborative Innovation Center of Chemistry for Life Sciences, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, 210023 China;2. The First Affiliated Hospital of Gannan Medical University, Ganzhou, 341000 China |
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| Abstract: | - 1.1. The enzymatic nature of human liver, bone, placental and intestinal alkaline phosphatases (ALPs) were investigated with phosphorylcholine (PC), phosphoryl-ethanolamine, pyridoxal-5'-phosphate and p-nitrophenylphosphate at a weakly alkaline pH.
- 2.2. The apparent Km value of the intestinal ALP with PC was the highest of all ALPs tested. Intestinal ALP hydrolyzes PC the most and has higher affinity for choline as a transphorsphorylating acceptor than the other ALPs. In addition, the intestinal ALP activity with PC was most susceptible to Na2HPO4, in the tested ALPs.
- 3.3. The present results suggest that PC is a unique substrate for human intestinal ALP, which may be related to the metabolism of PC or choline as part of phosphatidylcholine.
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