Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1969 Jan;62(1):128–135. doi: 10.1073/pnas.62.1.128

RATES OF POLYPEPTIDE CHAIN ASSEMBLY IN LIVER IN VIVO: RELATION TO THE MECHANISM OF TEMPERATURE ACCLIMATION IN OPSANUS TAU*

Audrey E V Haschemeyer 1,2
PMCID: PMC285964  PMID: 5253648

Abstract

A simple translational model, present herein, permits experimental determination of the rates of protein synthesis in vivo in terms of a time constant representing the average assembly time of the polypeptide chains. The model has been used to interpret incorporation of radioactive amino acids into toadfish liver fractions as a function of time after hepatic portal vein injection. The results suggest that the increase in liver protein synthesis produced by cold acclimation is due to a more rapid rate of addition of amino acid residues to the growing polypeptide chains. The finding is consistent with the greater aminoacyl transferase activity in livers of cold-acclimated fish.

Full text

PDF
128

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BOLLUM F. J. Thermal conversion of nonpriming deoxyribonucleic acid to primer. J Biol Chem. 1959 Oct;234:2733–2734. [PubMed] [Google Scholar]
  2. DINTZIS H. M. Assembly of the peptide chains of hemoglobin. Proc Natl Acad Sci U S A. 1961 Mar 15;47:247–261. doi: 10.1073/pnas.47.3.247. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. FESSENDEN J. M., MOLDAVE K. Studies on amino acyl transfer from soluble-RNA to rat liver ribonucleoprotein particles; effect of soluble and microsomal extracts. Biochemistry. 1962 May 25;1:485–490. doi: 10.1021/bi00909a019. [DOI] [PubMed] [Google Scholar]
  4. FESSENDEN J. M., MOLDAVE K. Studies on aminoacyl transfer from soluble ribonucleic acid to ribosomes. Resolution of two soluble transferring activities. J Biol Chem. 1963 Apr;238:1479–1484. [PubMed] [Google Scholar]
  5. FREED J. CHANGES IN ACTIVITY OF CYTOCHROME OXIDASE DURING ADAPTATION OF GOLDFISH TO DIFFERENT TEMPERATURES. Comp Biochem Physiol. 1965 Apr;14:651–659. doi: 10.1016/0010-406x(65)90252-5. [DOI] [PubMed] [Google Scholar]
  6. HOFMANN T., HARRISON P. M. The structure of apoferritin: degradation into and molecular weight of subunits. J Mol Biol. 1963 Apr;6:256–267. doi: 10.1016/s0022-2836(63)80087-x. [DOI] [PubMed] [Google Scholar]
  7. Haschemeyer A. E. Compensation of liver protein synthesis in temperature-acclimated toadfish, Opsanus tau. Biol Bull. 1968 Aug;135(1):130–140. doi: 10.2307/1539620. [DOI] [PubMed] [Google Scholar]
  8. Hunt T., Hunter T., Munro A. Control of haemoglobin synthesis: distribution of ribosomes on the messenger RNA for alpha and beta chains. J Mol Biol. 1968 Aug 28;36(1):31–45. doi: 10.1016/0022-2836(68)90217-9. [DOI] [PubMed] [Google Scholar]
  9. LOFTFIELD R. B., EIGNER E. A. The time required for the synthesis of a ferritin molecule in rat liver. J Biol Chem. 1958 Apr;231(2):925–943. [PubMed] [Google Scholar]
  10. Skogerson L., Moldave K. Evidence for aminoacyl-tRNA binding, peptide bond synthesis, and translocase activities in the aminoacyl transfer reaction. Arch Biochem Biophys. 1968 May;125(2):497–505. doi: 10.1016/0003-9861(68)90607-3. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES