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Interactions between lipopolysaccharide and outer membrane proteins of Acinetobacter calcoaceticus studied by an affinity electrophoresis system
Author(s) -
Borneleit Petra,
Blechschmidt Bernd,
Kleber HansPeter
Publication year - 1989
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150100403
Subject(s) - acinetobacter calcoaceticus , lipopolysaccharide , bacterial outer membrane , dissociation constant , chemistry , dissociation (chemistry) , membrane , affinity electrophoresis , membrane protein , chromatography , polyacrylamide gel electrophoresis , electrophoresis , biochemistry , affinity chromatography , biophysics , biology , receptor , escherichia coli , organic chemistry , enzyme , acinetobacter , gene , endocrinology , antibiotics
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 M r 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.