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利用亲和电泳系统研究醋酸钙不动杆菌脂多糖与外膜蛋白之间的相互作用。

Interactions between lipopolysaccharide and outer membrane proteins of Acinetobacter calcoaceticus studied by an affinity electrophoresis system.

作者信息

Borneleit P, Blechschmidt B, Kleber H P

机构信息

Sektion Biowissenschaften, Karl-Marx-Universität, Leipzig.

出版信息

Electrophoresis. 1989 Apr;10(4):234-7. doi: 10.1002/elps.1150100403.

DOI:10.1002/elps.1150100403
PMID:2743966
Abstract

R-Form lipopolysaccharides of Acinetobacter calcoaceticus could be incorporated into polyacrylamide gels in an immobile form by adding it directly to the acrylamide-N,N'-methylenebisacrylamide polymerization mixture. The separation of A. calcoaceticus 69 V outer membrane proteins in these affinity gels demonstrated a specific interaction with the lipopolysaccharide ligand for one of the proteins. This protein is heat-modifiable and has an Mr of about 18,000. By incorporation of varying concentrations of lipopolysaccharide, a dissociation constant of the protein-lipopolysaccharide complex of 0.5 mM could be determined. In comparison, for another A. calcoaceticus strain, CCM 5593, a higher dissociation constant (1.0 mM)--indicative of lower affinity--was obtained.

摘要

通过将醋酸钙不动杆菌的R型脂多糖直接添加到丙烯酰胺-N,N'-亚甲基双丙烯酰胺聚合混合物中,它可以以固定形式掺入聚丙烯酰胺凝胶中。在这些亲和凝胶中对醋酸钙不动杆菌69 V外膜蛋白的分离表明,其中一种蛋白与脂多糖配体存在特异性相互作用。这种蛋白可被热修饰,分子量约为18,000。通过掺入不同浓度的脂多糖,可以确定蛋白-脂多糖复合物的解离常数为0.5 mM。相比之下,对于另一株醋酸钙不动杆菌CCM 5593,获得了更高的解离常数(1.0 mM),这表明其亲和力较低。

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