Purification and characterization of lipopolysaccharide‐binding protein from hemolymph of American cockroach Periplaneta americana
- 1 May 1990
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 190 (1), 201-206
- https://doi.org/10.1111/j.1432-1033.1990.tb15565.x
Abstract
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 homoligomer 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+.This publication has 40 references indexed in Scilit:
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