Purification of Escherichia coli 50 S ribosomal proteins by high performance liquid chromatography

FEBS Letters

Kamp, Roza Maria¹  Wittmann-Liebold, Brigitte¹ 

[1] Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, D-1000 Berlin 33 (Dahlem), FRG

关键词: Escherichia coli ribosome;    50 S subunit protein;    High performance liquid chromatography;    Protein recovery;    Micro-sequencing;   

DOI  :  10.1016/0014-5793(84)80832-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The 50 S subunit proteins from the Escherichia coli ribosome were purified by size-exclusion, ion-exchange or reversed phase high performance liquid chromatography (HPLC) avoiding any precipitation or desalting procedures during isolation. Best resolution of this complex protein mixture was achieved by reversed phase chromatography on supports with short alkyl chains and C18 hydrocarbon-bonded phases; 23 out of the 32 proteins from the 50 S subunit were purified as shown by two-dimensional gel electrophoresis, amino acid analysis and direct micro-sequencing. Protein recoveries varied between 25 and 84% as determined by amino acid analysis. Ribosomal proteins of other organims can be separated under similar conditions.

【 授权许可】

Unknown