title: Identification of Treponema pallidum penicillin-binding proteins.
abstract: Penicillin-binding proteins of 180, 89, 80, 68, 61, 41, and 38 kilodaltons were identified in Treponema pallidum (Nichols) by their covalent binding of [35S]benzylpenicillin. Penicillin-binding proteins are localized in the plasma membranes of many bacterial species and may serve as useful markers for determining plasma membrane intactness in T. pallidum fractionation studies.
authors.affiliation: Department of Microbiology and Immunology, School of Medicine, University of California, Los Angeles 90024.
authors.forename: T M
authors.initials: TM
authors.lastname: Cunningham
authors.forename: J N
authors.initials: JN
authors.lastname: Miller
authors.forename: M A
authors.initials: MA
authors.lastname: Lovett
mesh_terms: D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006602:Hexosyltransferases; D008970:Molecular Weight; D002267:Muramoylpentapeptide Carboxypeptidase / Q000302:isolation & purification* / Q000378:metabolism; D010400:Penicillin G / Q000378:metabolism*; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D014210:Treponema pallidum / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase; D010400:Penicillin G