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

被引：0
|
作者：
R. Salazar
R. Brandt
J. Kellermann
S. Krantz
机构：
[1] Ernst-Moritz-Arndt-Universität,Institut für Medizinische Biochemie und Molekularbiologie
[2] Klinikum Sauerbruchstraße,undefined
[3] Max-Planck-Institut für Biochemie,undefined
来源：
Glycoconjugate Journal | 2000年 / 17卷
关键词：
glycation; fructosyllysine; receptor; cellular myosin heavy chain; nucleolin;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
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.
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页码：713 / 716
页数：3
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