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Purification and multiple forms of human placental alkaline phosphatase
Authors:G G Chang  T C Chang  F Pan
Institution:1. College of Biology and Environmental Engineering, Zhejiang Shuren University, Hangzhou, 310015, PR China;2. Institute of Quality and Standard for Agriculture Products, Zhejiang Academy of Agricultural Science, Hangzhou, 310021, PR China;3. School of Food Science and Technology, Jiangnan University, Wuxi 214122, PR China;1. Key Laboratory of Functional Dairy, College of Food Science and Nutritional Engineering, China Agricultural University, No.17 Qinghua East Road, Haidian District, Beijing 100083, PR China;2. College of Agriculture and Biotechnology, China Agricultural University, No.2 Yuanmingyuan West Road, Haidian District, Beijing 100193, PR China;3. Ausnutria Hyproca Dairy Group BV, No.2 Wangwang East Road, Wangcheng District, Changsha 410200, PR China;1. Department of Soil Sciences and Agri-Food Engineering, Université Laval, Quebec, Qc G1V 0A6, Canada;2. School of Nutrition Sciences, Faculty of Health Sciences, University of Ottawa, Ottawa, Ontario, Canada;3. Institute of Nutrition and Functional Foods (INAF), Université Laval, Quebec, Qc G1V 0A6, Canada
Abstract:The commercially available human placental alkaline phosphatase was purified to near homogeneity. Multiple bands of the purified enzyme were resolved in the polyacrylamide gel. The number of bands in the gel was reduced after the enzyme was treated with neuraminidase.
Keywords:
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