Acylated proteins in Borrelia hermsii, Borrelia parkeri, Borrelia anserina, and Borrelia coriaceae.
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.
Sambri
V
V
Institute of Microbiology, St. Orsola Hospital, Bologna, Italy.
Stefanelli
C
C
Rossoni
C
C
La Placa
M
M
Cevenini
R
R
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
D001426:Bacterial Proteins; D005227:Fatty Acids; D008074:Lipoproteins