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Regulation of translation in rabbit reticulocytes and mouse L‐cells; comparison of the effects of temperature
Author(s) -
Craig Nessly
Publication year - 1976
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1040870204
Subject(s) - polysome , mole , elongation , protein biosynthesis , translation (biology) , chemistry , activation energy , biochemistry , messenger rna , biophysics , biology , microbiology and biotechnology , rna , ribosome , materials science , ultimate tensile strength , metallurgy , gene
Various parameters of protein synthesis were analyzed in rabbit reticulocytes exposed to various temperatures for up to five hours. Between 10°C and 40°C total protein synthesis exhibited two different apparent activation energies (36 kcal/mole, 10–24°C; 22 kcal/mole, 24–40°C), as did protein elongation and release (35 kcal/mole, 10–25°C; 12 kcal/mole, 25–40°C). However, the level of polysomes remained essentially unchanged between 0°C and 42°C which implies that the activation energy for polypeptide initiation is quite similar to that for elongation and is also biphasic. This situation is different from that in cultured mouse L‐cells where the polysome level is dependent on temperatures. Nevertheless, reticulocytes and L‐cells appear to be similar in their temperature dependence of initiation and in their rate of elongation (5–6 amino acids/second at 36°C).