Isolation of eukaryotic ribosomal proteins. Purification and characterization of 60 S ribosomal subunit proteins L3, L6, L7', L8, L10, L15, L17, L18, L19, L23', L25, L27', L28, L29, L31, L32, L34, L35, L36, L36', and L37'.
نویسندگان
چکیده
منابع مشابه
The 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 کاملRibosome conformational changes associated with protein S6 phosphorylation.
The relative accessibility of rat liver ribosomal proteins to reductive methylation was examined using ribosomes with unphosphorylated, and extensively phosphorylated S6. Comparison of the results indicated that proteins S3, S4, S7, and S23/24 of the small subunit, and proteins L9, L10, L12, L18, L27, L34, and L36 are involved in a ribosomal conformational change.
متن کاملIdentification by affinity chromatography of the eukaryotic ribosomal proteins that bind to 5.8 S ribosomal ribonucleic acid.
The proteins that bind to rat liver 5.8 S ribosomal ribonucleic acid were identified by affinity chromatography. The nucleic acid was oxidized with periodate and coupled by its 3'-terminus to Sepharose 4B through and adipic acid dihydrazide spacer. The ribosomal proteins that associate with the immobilized 5.8 S rRNA were identified by polyacrylamide gel electrophoresiss: they were L19, L8, and...
متن کاملImmobilized eukaryotic 5.8 S RNA binds Escherichia coli and rat liver ribosomal proteins.
The eukaryotic ribosome contains two lowmolecular weight RNAs, 5 S RNA and 5.8 S RNA (for reviews [ 1,2]). The larger species is specific only for eukaryotic ribosome and, like 5 S RNA, is a component of the large subunit. Earlier we found that the immobilized rat liver 5.8 S RNA forms a complex with 60 S subunit proteins L.5, L6, L7 and L18 [3]. The yeast 5.8 S RNA has been shown to interact a...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1977
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)40344-9