Effects of lipopolysaccharide chemotype structure on binding and inactivation of hen egg lysozyme

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Abstract
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°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.

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