Identification by affinity chromatography of the rat liver ribosomal proteins that bind to Escherichia coli 5 S ribosomal ribonucleic acid.
نویسندگان
چکیده
The eukaryotic and prokaryotic ribosomal proteins that bind to Escherichia coli 5 S rRNA were identified by affinity chromatography. The E. coli ribosomal proteins that associated with the nucleic acid were L5, L18, and L25 confirming earlier findings using the same and different procedures. The rat liver ribosomal proteins that associated with E. coli 5 S rRNA were L6, L7, L19, L35a, and S9; several of those proteins also bind to rat liver 5 S rRna (L6, L19) and to 5.8 S rRna (L6, L19, and S9).
منابع مشابه
Identification 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...
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...
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Mixed yeast elongator-tRNAs (bulk tRNA lacking fRNAm,fMet), pure isoaccepting species of elongator-tRNAs (tRNAmMet and tRNAPhe), and purified initiator-tRNA (tRNAfMet) were each oxidized with periodate and the 3' terminus was coupled to Sepharose 4B through an adipic acid dihydrazide spacer. The rat liver ribosomal proteins that associated with the tRNAs were isolated by affinity chromatography...
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متن کاملThe binding of transfer ribonucleic acids to 5 S and 5.8 S eukaryotic ribosomal ribonucleic acid-protein complexes.
Rat liver 5 S and 5.8 S rRNAs were oxidized with periodate and the 3' termini were coupled to Sepharose 4B through an adipic acid dihydrazide spacer. Ribosomal proteins were passed through the nucleic acid affinity columns to form ribonucleoprotein complexes containing the nucleic acid and the proteins that bind to it (5 S . L6, L7, L19; and 5.8 S . L6, L19, S9, S13). Pure isoaccepting species ...
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 255 2 شماره
صفحات -
تاریخ انتشار 1980