Article

Glycoconjugate Journal

, Volume 17, Issue 10, pp 713-716

First online:

Purification and characterization of a 200[emsp4 ]kDa fructosyllysine-specific binding protein from cell membranes of U937 cells

  • R. SalazarAffiliated withInstitut für Medizinische Biochemie und Molekularbiologie, Ernst-Moritz-Arndt-Universität, Klinikum Sauerbruchstraße
  • , R. BrandtAffiliated withInstitut für Medizinische Biochemie und Molekularbiologie, Ernst-Moritz-Arndt-Universität, Klinikum Sauerbruchstraße
  • , J. KellermannAffiliated withMax-Planck-Institut für Biochemie
  • , S. KrantzAffiliated withInstitut für Medizinische Biochemie und Molekularbiologie, Ernst-Moritz-Arndt-Universität, Klinikum Sauerbruchstraße

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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 100[emsp4 ]kDa were isolated. MS-analysis of the 200[emsp4 ]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.

glycation fructosyllysine receptor cellular myosin heavy chain nucleolin