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Nature of the relationship between vitamin B12 binding and cell uptake
Authors:A E Finkler  C A Hall
Affiliation:1. Department of Neurobiology, School of Medicine, Kangwon National University, Chuncheon 200-701, South Korea;2. Department of Neuroscience, College of Medicine, Korea University, Seoul 136-705, South Korea;3. Department of Physiology, College of Medicine, Institute of Neurodegeneration and Neuroregeneration, Hallym University, Chuncheon 200-702, South Korea;4. Department of Biomedical Science,Research Institute for Bioscience and Biotechnology, Hallym University, Chuncheon 200-702, South Korea;5. Department of Emergency Medicine, School of Medicine, Kangwon National University, Chuncheon 200-701, South Korea;6. Department of Emergency Medicine, Sacred Heart Hospital, College of Medicine, Hallym University, Anyang 431-796, South Korea;7. Department of Emergency Medicine, Chuncheon Sacred Heart Hospital, College of Medicine, Hallym University, Chuncheon 200-702, South Korea;8. Department of Pediatrics, Chuncheon Sacred Heart Hospital, College of Medicine, Hallym University, Chuncheon 200-701, South Korea;9. Department of Occupational Therapy, Dongnam Health College, Suwon 440-714, South Korea;10. Department of Molecular and Cellular Biochemistry, School of Medicine, Kangwon National University, Chuncheon 200-701, South Korea
Abstract:Transcobalamin II was shown to be a specific B12 transport protein promoting the uptake of B12 by human normal and malignant cells. Transcobalamin I, the other known transport protein, and the B12 binding substances of erythrocytes, leukocytes, saliva, and gastric juice, did not enhance the uptake of B12 by tissue cells in vitro. Transcobalamin II was strongly retained on carboxymethyl-cellulose, but the other B12 binders passed through with the equilibrium buffer. After uptake by human tumor cells a transcobalamin II-B12 complex was changed into a macromolecule that had the chromatographic characteristics of transcobalamin I.
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