Binding of aminoacyl-tRNA to rat liver ribosomal proteins
β Scribed by Ramon Reyes; Luis Carrasco; David Vazquez
- Publisher
- Springer
- Year
- 1976
- Tongue
- English
- Weight
- 272 KB
- Volume
- 2
- Category
- Article
- ISSN
- 0301-4851
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β¦ Synopsis
Rat liver ribosome treatment with ethanol and 1 M NH4Cl releases some 31-33 ribosomal proteins. This split protein fraction binds Phe-tRNA, Ac-Phe-tRNA, Met-tRNAM and f-Met-tRNAF in the absence of K+ and Mg++ ions. When the split protein fraction is passed through Sephadex G-100 only six proteins are retained in the column: S10, S14, S15, S19, L35, and L36. The aminoacyl-tRNA binding activity of this protein fraction retained in the Sephadex G-100 column is similar to that of the total split protein fraction, suggesting that the above six proteins, or only some of them, are involved in the binding reaction.
π SIMILAR VOLUMES
Aminoacyl-tRNA synthetases from rat-liver cytoplasm were fractionated into two groups, characterized by their sedimentation coefficients of about 20S and 5S, respectively. These two groups of synthetases could be isolated from postmicrosomal supernatant either by gradient centrifugation, by gel filt
## Abstract Ricin A chain was radioactively labeled using reductive alkylation, lactoperoxidase catalyzed iodination, and reaction with iodoacetamide or Nβethylmaleimide (NEM). The inhibition of cellβfree rat liver protein synthesis by the modified A chains and the ribosome binding characteristics