Identification by affinity chromatography of Escherichia coli ribosomal proteins that bind erythromycin and chloramphenicol.
Erythromycin and chloramphenicol have been coupled to epoxy-activated Sepharose-6B. Extracted ribosomal proteins from 30S and 50S ribosomal subunits of Escherichia coli have been chromatographed on the coupled columns under reconstitution buffer conditions. Proteins bound to the columns were recovered and identified by two-dimensional polyacrylamide gel electrophoresis. Proteins L4, L5 and L21 bound to both columns. Proteins S5 and S7 showed weak binding to erythromycin-Sepharose.
D002701:Chloramphenicol / Q000378:metabolism*; D002846:Chromatography, Affinity / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D004917:Erythromycin / Q000378:metabolism*; D004926:Escherichia coli / Q000032:analysis*; D011485:Protein Binding; D012269:Ribosomal Proteins / Q000302:isolation & purification* / Q000378:metabolism
D012269:Ribosomal Proteins; D004917:Erythromycin; D002701:Chloramphenicol