Rates of polypeptide chain assembly in liver in vivo: relation to the mechanism of temperature acclimation in Opsanus tau.
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.
D000064:Acclimatization; D000818:Animals; D005399:Fishes / Q000378:metabolism*; D008099:Liver / Q000201:enzymology* / Q000502:physiology*; D008433:Mathematics; D008954:Models, Biological; D010452:Peptide Biosynthesis; D014176:Protein Biosynthesis; D013995:Time; D000637:Transaminases / Q000378:metabolism*
D000637:Transaminases