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

Abstract:

: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 organisms can be separated under similar conditions.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Kamp RM,Wittmann-Liebold B

doi

10.1016/0014-5793(84)80832-7

subject

Has Abstract

pub_date

1984-02-13 00:00:00

pages

59-63

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(84)80832-7

journal_volume

167

pub_type

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