Detection of a gonococcal endo-β-N-acetyl-D-glucosaminidase and its peptidoglycan cleavage site

Abstract

N. gonorrhoeae contains several hydrolases which may be responsible for gonococcal cell lysis. One of these enzymes, an endo-β-N-acetyl-D-glucosaminidase, has been extracted from supernatants of sonicated gonococci and partially purified by ammonium sulfate precipitation and affinity and ion-exchange chromatography. This enzyme has a different specificity than egg white lysozyme and cleaves the β 1→4 glycosidic linkage between N-acetylglucosamine and N-acetylmuramic acid in gonococcal peptidoglycan.