Molecular Biology Reports

, Volume 9, Issue 4, pp 219–222 | Cite as

Affinity labelling of rat liver ribosomal protein S26 by heptauridylate containing a 5′-terminal alkylating group

  • J. Stahl
  • N. D. Kobetz


Heptauridylate bearing a radioactive alkylating [14C]-4-(N-2-chloroethyl-N-methylamino)benzylamine attached to the 5′-phosphate via amide bond, was bound to ribosomes and small ribosomal subunits from rat liver which thereby were coded to bind N-acylated Phe tRNA. After completion of the alkylating reaction and subsequent hydrolysis of the phosphamide bond ribosomal proteins were isolated. Radioactivity was found covalently associated preferentially with protein S26 and, to a very small extent, with proteins S3 and S3a. The affinity labelling reaction could be abolished by (pU)14 and poly(U). From the results it is concluded that ribosomal protein S26 is located at the mRNA binding site of rat liver ribosomes.


Phosphate Amide Binding Site Ribosomal Protein Small Extent 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Dr W. Junk Publishers 1984

Authors and Affiliations

  • J. Stahl
    • 1
  • N. D. Kobetz
    • 2
  1. 1.Department of Cell PhysiologyCentral Institute of Molecular Biology, Academy of Sciences of the GDRBerlin-BuchGDR
  2. 2.Institute of Organic ChemistrySiberian Branch of the Academy of Sciences of the USSRNovosibirskUSSR

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