title: Purification and characterization of the autolytic glycosidase of Streptococcus pneumoniae.
abstract: A new lytic enzyme isolated from Streptococcus pneumoniae has been purified to electrophoretical homogeneity. The enzyme, showing a Mr of 64000, has been characterized as an endo-beta-1,4-N-acetylglucosaminidase that requires choline in the teichoic acid of the cell wall substrate for catalytic activity. In vivo experiments demonstrate that the glucosaminidase behaves as an autolytic enzyme.
authors.affiliation: Centro de Investigaciones Biológicas, C.S.I.C., Madrid, Spain.
authors.forename: P
authors.initials: P
authors.lastname: García
authors.forename: J L
authors.initials: JL
authors.lastname: García
authors.forename: E
authors.initials: E
authors.lastname: García
authors.forename: R
authors.initials: R
authors.lastname: López
mesh_terms: D000118:Acetylglucosaminidase / Q000302:isolation & purification* / Q000378:metabolism; D001329:Autolysis; D002846:Chromatography, Affinity; D006596:Hexosaminidases / Q000302:isolation & purification*; D007700:Kinetics; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D008970:Molecular Weight; D013296:Streptococcus pneumoniae / Q000201:enzymology*; D014461:Ultracentrifugation
chemical_list: D006596:Hexosaminidases; D000118:Acetylglucosaminidase; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase