Purification and characterization of lipopolysaccharide-binding protein from hemolymph of American cockroach Periplaneta americana.
A protein having affinity to lipopolysaccharide of Escherichia coli K12 was purified to homogeneity from the hemolymph of Periplaneta americana. This protein, with an average molecular mass of 450 kDa. was a homooligomer of a 28-kDa subunit protein. Comparative studies using lipopolysaccharide molecules of E. coli and Salmonella minnesota suggested that this protein recognizes and binds to a specific carbohydrate structure of E. coli lipopolysaccharide. Ca2+ was required for this protein to bind to lipopolysaccharide, but other divalent cations could not replace Ca2+.
Jomori
T
T
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Kubo
T
T
Natori
S
S
D000209:Acute-Phase Proteins; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002240:Carbohydrate Sequence; D002352:Carrier Proteins / Q000302:isolation & purification*; D003058:Cockroaches / Q000032:analysis*; D006458:Hemolymph / Q000032:analysis*; D015151:Immunoblotting; D008562:Membrane Glycoproteins; D008969:Molecular Sequence Data; D000099231:Lipopolysaccharide-Binding Protein
D000209:Acute-Phase Proteins; D000596:Amino Acids; D002352:Carrier Proteins; D008562:Membrane Glycoproteins; D000099231:Lipopolysaccharide-Binding Protein