Fast preparative separation of 'native' core E coli 30S ribosomal proteins.
We have developed an ion-exchange high performance liquid chromatographic method for preparative separation of 'core' proteins from E coli 30S ribosomal subunits, extracted with salt under non-denaturing conditions. This method yields individual proteins in pure and native form at high concentrations, (5 to 25 mg/ml) suitable for direct use in 1D-, 2D- or 3D-NMR studies.
Cachia
C
C
Laboratoire de Biophysique, UFR des Sciences Pharmaceutiques et Biologiques, Dijon, France.
Flamion
P J
PJ
Schreiber
J P
JP
D001426:Bacterial Proteins / Q000302:isolation & purification*; D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D002852:Chromatography, Ion Exchange / Q000379:methods; D004926:Escherichia coli / Q000737:chemistry; D012269:Ribosomal Proteins / Q000302:isolation & purification*
D001426:Bacterial Proteins; D012269:Ribosomal Proteins; C040469:ribosomal protein S30