Isolation of eukaryotic ribosomal proteins. Purification and characterization of the 60 S ribosomal subunit proteins L4, L5, L7, L9, L11, L12, L13, L21, L22, L23, L26, L27, L30, L33, L35', L37, and L39
نویسندگان
چکیده
منابع مشابه
Isolation of Eukaryotic Ribosomal Proteins
The proteins of the large subunit of rat liver ribosomes were separated into seven groups by stepwise elution from carboxymethylcellulose with LiCl at pH 6.5. Seventeen proteins (L4, L5, Li’, L9, Lll, L12, L13, L21, L22, L23, L26, L27, L30, L33, L35’, L37, and L39) were isolated from three of the groups (B60, D60, G60) by ion exchange chromatography on carboxymethylcellulose and by filtration t...
متن کاملIsolation of Eukaryotic Ribosomal Proteins
The proteins of the large subunit of rat liver ribosomes were separated into seven groups by stepwise elution from carboxymethylcellulose with LiCl at pH 6.5. Seventeen proteins (L4, L5, Li’, L9, Lll, L12, L13, L21, L22, L23, L26, L27, L30, L33, L35’, L37, and L39) were isolated from three of the groups (B60, D60, G60) by ion exchange chromatography on carboxymethylcellulose and by filtration t...
متن کاملThe large subunit of the mammalian mitochondrial ribosome. Analysis of the complement of ribosomal proteins present.
Identification of all the protein components of the large subunit (39 S) of the mammalian mitochondrial ribosome has been achieved by carrying out proteolytic digestions of whole 39 S subunits followed by analysis of the resultant peptides by liquid chromatography and mass spectrometry. Peptide sequence information was used to search the human EST data bases and complete coding sequences were a...
متن کاملProtein-protein cross-linking of the 50 S ribosomal subunit of Escherichia coli using 2-iminothiolane. Identification of cross-links by immunoblotting techniques.
We have investigated the protein-protein cross-links formed within the 50 S subunit of the Escherichia coli ribosome using 2-iminothiolane as the cross-linking reagent. The members of the cross-links have been identified by immunoblotting from one-dimensional and two-dimensional diagonal sodium dodecyl sulfate-polyacrylamide gels using antisera specific for the individual ribosomal proteins. Th...
متن کاملIdentification by affinity chromatography of the eukaryotic ribosomal proteins that bind to 5 S ribosomal ribonucleic acid.
Rat liver 5 S ribosomal RNA was oxidized with periodate and coupled by its 3' terminus to Sepharose 4B through an adipic acid dihydrazide spacer. The ribosomal proteins that bind to that nucleic acid were isolated by affinity chromatography and identified by electrophoresis in polyacrylamide gels. The eukaryotic 5 S rRNA binding proteins were L6 and L19: small amounts of L7, L23', L27/L27', L35...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1976
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)57023-5