Abstract
Peptidoglycan was isolated from Bacteroides fragilis with boiling sodium dodecyl sulfate, and some was treated with pronase to eliminate contaminating protein. This peptidoglycan was chemotactic for rabbit polymorphonuclear neutrophils and had even greater chemotactic activity along with some chemokinetic activity after it was partially hydrolyzed with lysozyme. Significant chemotaxis-inhibitory activity was observed for an acid-precipitable component of the lysozyme-treated crude peptidoglycan of B. fragilis.
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