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

Authors
Salazar, R Brandt, R Kellermann, J Krantz, S
Citation
R. Salazar et al., Purification and characterization of a 200 kDa fructosyllysine-specific binding protein from cell membranes of U937 cells, GLYCOCON J, 17(10), 2000, pp. 713-716
Citations number
10
Categorie Soggetti
Biochemistry & Biophysics
Journal title
GLYCOCONJUGATE JOURNAL
ISSN journal
02820080 → ACNP
Volume
17
Issue
10
Year of publication
2000
Pages
713 - 716
Database
ISI
SICI code
0282-0080(200010)17:10<713:PACOA2>2.0.ZU;2-C
Abstract
Amadori-modified proteins are bound by macrophages and monocytes via fructo syllysine-specific receptors. Detergent extracts from U937 cell membranes w ere used to purify the binding proteins by affinity purification on glycate d polylysine coated magnetic beads followed by SDS-PAGE. Two proteins of 20 0 and 100 kDa were isolated. MS-analysis of the 200 kDa protein showed high homologies with cellular myosin heavy chain, type A. Both fructosyllysine specific binding proteins, cellular myosin heavy chain and nucleolin, are g lycosylated.