Effects of lipopolysaccharide chemotype structure on binding and inactivation of hen egg lysozyme.
The structural features of lipopolysaccharide [LPS] which influence the binding and inactivation of lysozyme have been examined. Binding of polysaccharide-containing LPS (S-LPS) and Ra-Rc-LPS preparations was independent of temperature between 37-50 degrees C; in contrast, binding of Rd-LPS, Re-LPS and lipid A was temperature-dependent. The binding of lysozyme to Rd-LPS and Re-LPS was increased by treatment with mild alkali, which has little detectable effect on binding of lysozyme to S-LPS and Ra-Rc-LPS preparations. Competitive binding experiments using dansylated lysozyme and/or dansylated polymyxin B indicated independent binding sites on the LPS for lysozyme and polymyxin B. These results indicate significant differences between most LPS preparations and lipid A and glycolipid LPS in their interaction with proteins of mammalian origin.
Ohno
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N
Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City.
Morrison
D C
DC
D000818:Animals; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002645:Chickens; D004926:Escherichia coli / Q000276:immunology; D005260:Female; D007700:Kinetics; D008070:Lipopolysaccharides / Q000302:isolation & purification / Q000494:pharmacology*; D008969:Molecular Sequence Data; D009113:Muramidase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D011485:Protein Binding; D012475:Salmonella / Q000276:immunology; D013329:Structure-Activity Relationship
D008070:Lipopolysaccharides; D009113:Muramidase