Glycoconjugate Journal

, Volume 17, Issue 10, pp 713–716

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

Authors

  • R. Salazar
    • Institut für Medizinische Biochemie und MolekularbiologieErnst-Moritz-Arndt-Universität, Klinikum Sauerbruchstraße
  • R. Brandt
    • Institut für Medizinische Biochemie und MolekularbiologieErnst-Moritz-Arndt-Universität, Klinikum Sauerbruchstraße
  • J. Kellermann
    • Max-Planck-Institut für Biochemie
  • S. Krantz
    • Institut für Medizinische Biochemie und MolekularbiologieErnst-Moritz-Arndt-Universität, Klinikum Sauerbruchstraße
Article

DOI: 10.1023/A:1011074705615

Cite this article as:
Salazar, R., Brandt, R., Kellermann, J. et al. Glycoconj J (2000) 17: 713. doi:10.1023/A:1011074705615

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.

glycationfructosyllysinereceptorcellular myosin heavy chainnucleolin

Copyright information

© Kluwer Academic Publishers 2000