Purification and characterization of rabbit haptocorrin |
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| Affiliation: | 1. Department of Laboratory Medicine, Hospital Universitari Son Espases, Palma, Spain;2. Institut d́Investigació Sanitària de les Illes Balears (IdISBa), Spain;1. Nutristasis Unit, Viapath, Guy’s and St. Thomas'' Hospital NHS Trust, London, United Kingdom;2. Faculty of Life Sciences and Medicine, King''s College London, United Kingdom;3. Laboratory Corporation of America Holdings, Elon, USA;4. Viapath Informatics, London, United Kingdom;5. Department of Psychiatry, University of Cambridge, Cambridge, United Kingdom;6. Biochemical Medicine, King''s College London, United Kingdom;7. Guy’s and St. Thomas’ Hospital NHS Trust and Lewisham and Greenwich NHS Trust, London, United Kingdom;1. Department of Clinical Biochemistry, Regional Hospital Horsens, Sundvej 30, 8700 Horsens, Denmark;2. Department of Clinical Biochemistry, Aarhus University Hospital, Palle Juul-Jensens Boulevard 99, 8200 Aarhus N, Denmark |
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| Abstract: | Rabbit haptocorrin (R-binder) has been purified from serum by affinity chromatography on cobalamin-Sepharose and Blue Sepharose. It proved to be a protein with a relative molecular mass of 60 000 and an amino acid content very similar to that of other haptocorrins (Nexø, E. and Olesen, H. (1981) in B12 (Dolphin, D., ed.), Wiley Interscience, New York/London, in the press). The pH optimum (pH 6–9) for binding of cyanocobalamin and the affinity to dicyanocobinamide were like those of human and hog haptocorrins. In spectral studies, the extinction coefficient of cyanocobalamin at 363 nm (γ1-band) increased by about 16% on binding to rabbit haptocorrin. Binding of azidocobalamin gave spectra changes similar to those for binding to rabbit transcobalamin. |
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