title: Acylated proteins in Borrelia hermsii, Borrelia parkeri, Borrelia anserina, and Borrelia coriaceae.
abstract: Borrelia hermsii, Borrelia parkeri, Borrelia anserina, and Borrelia coriaceae produced several lipoproteins identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography of bacteria grown in [3H]palmitate. Five major acylated proteins were demonstrated by sequential alkaline and acid hydrolysis. High-pressure liquid chromatography of isolated proteins confirmed that covalently bound radioactivity was represented by fatty acids.
authors.affiliation: Institute of Microbiology, St. Orsola Hospital, Bologna, Italy.
authors.forename: V
authors.initials: V
authors.lastname: Sambri
authors.forename: C
authors.initials: C
authors.lastname: Stefanelli
authors.forename: C
authors.initials: C
authors.lastname: Rossoni
authors.forename: M
authors.initials: M
authors.lastname: La Placa
authors.forename: R
authors.initials: R
authors.lastname: Cevenini
mesh_terms: D000215:Acylation; D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000302:isolation & purification; D001898:Borrelia / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005227:Fatty Acids / Q000032:analysis; D008074:Lipoproteins / Q000096:biosynthesis* / Q000737:chemistry / Q000302:isolation & purification; D008970:Molecular Weight; D013045:Species Specificity
chemical_list: D001426:Bacterial Proteins; D005227:Fatty Acids; D008074:Lipoproteins