Purification and characterization of a 200[emsp4 ]kDa fructosyllysine-specific binding protein from cell membranes of U937 cells |
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| Authors: | R Salazar R Brandt J Kellermann S Krantz |
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| Institution: | (1) Institut für Medizinische Biochemie und Molekularbiologie, Ernst-Moritz-Arndt-Universität, Klinikum Sauerbruchstraße, D-17487 Greifswald, Germany;(2) Max-Planck-Institut für Biochemie, Am Klopferspitz 1, D-82152 Martinsried, Germany |
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| Abstract: | Amadori-modified proteins are bound by macrophages and monocytes via fructosyllysine-specific receptors. Detergent extracts from U937 cell membranes were used to purify the binding proteins by affinity purification on glycated polylysine coated magnetic beads followed by SDS-PAGE. Two proteins of 200 and 100emsp4 ]kDa were isolated. MS-analysis of the 200emsp4 ]kDa protein showed high homologies with cellular myosin heavy chain, type A. Both fructosyllysine specific binding proteins, cellular myosin heavy chain and nucleolin, are glycosylated. |
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| Keywords: | glycation fructosyllysine receptor cellular myosin heavy chain nucleolin |
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