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从U937细胞膜中纯化和鉴定一种200 kDa的果糖基赖氨酸特异性结合蛋白。

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

作者信息

Salazar R, Brandt R, Kellermann J, Krantz S

机构信息

Institut für Medizinische Biochemie und Molekularbiologie, Ernst-Moritz-Arndt-Universität, Greifswald, Germany.

出版信息

Glycoconj J. 2000 Oct;17(10):713-6. 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 100kDa 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 glycosylated.

摘要

经阿马多里修饰的蛋白质通过果糖基赖氨酸特异性受体与巨噬细胞和单核细胞结合。利用U937细胞膜的去污剂提取物,通过在糖化聚赖氨酸包被的磁珠上进行亲和纯化,随后进行SDS-PAGE,来纯化结合蛋白。分离出了两种分子量分别为200 kDa和100 kDa的蛋白质。对200 kDa蛋白质的质谱分析显示,其与A型细胞肌球蛋白重链具有高度同源性。两种果糖基赖氨酸特异性结合蛋白,即细胞肌球蛋白重链和核仁素,均被糖基化。

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