CELL-FREE INCORPORATION OF AMINO ACIDS BY A TROUT-LIVER SYSTEM. HEAT-LABILE AMINOACYL TRANSFERASE ACTIVITY
- 1 December 1967
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry
- Vol. 45 (12) , 2005-2014
- https://doi.org/10.1139/o67-234
Abstract
A cell-free system from trout liver that incorporates amino acids into protein has been isolated. The system requires both soluble and particulate fractions, and is similar to those isolated from other organisms.The incorporation of amino acids is extremely heat-labile, and this lability has been localized in the aminoacyl transferase activity of the cell sap. The heat lability of the microsomes may also be related to transferase activity.Ribosomal fractions from trout liver and rat liver incorporate amino acids when incubated with cell sap from rat liver and trout liver, respectively.This publication has 21 references indexed in Scilit:
- Separation of three microbial amino acid polymerization factors.Proceedings of the National Academy of Sciences, 1966
- Protein SynthesisAnnual Review of Biochemistry, 1966
- Comparison of guanosine triphosphate split and polypeptide synthesis with a purified E. coli system.Proceedings of the National Academy of Sciences, 1966
- Nucleic Acids and Protein BiosynthesisAnnual Review of Biochemistry, 1965
- MECHANISM OF PEPTIDE BOND FORMATION IN POLYPEPTIDE SYNTHESISProceedings of the National Academy of Sciences, 1964
- RESOLUTION OF THE E. COLI AMINO ACYL sRNA TRANSFER FACTOR INTO TWO COMPLEMENTARY FRACTIONSProceedings of the National Academy of Sciences, 1964
- Ribosomal Aggregate Engaged in Protein Synthesis: Characterization of the ErgosomeNature, 1963
- Measurement of the incorporation of radioactive amino acids into protein by a filter-paper disk methodArchives of Biochemistry and Biophysics, 1961
- Factors determining the specificity of hemoglobin synthesized in a cell-free systemJournal of Molecular Biology, 1961
- THE SYNTHESIS OF HEMOGLOBIN IN A CELL-FREE SYSTEMProceedings of the National Academy of Sciences, 1958