Physiology of rat-liver polysomes: protein synthesis by stable polysomes

SH Wilson, HZ Hill, MB Hoagland - Biochemical Journal, 1967 - ncbi.nlm.nih.gov
SH Wilson, HZ Hill, MB Hoagland
Biochemical Journal, 1967ncbi.nlm.nih.gov
Certain qualitative aspects of protein synthesis in the livers of starved, starved–re-fed and
actinomycin D-treated rats have been examined by polyacrylamide-gel electrophoresis.
Animals were exposed to a mixture of 14 C-labelled acids for 18–20min. and killed, and an
ultrasonic extract of newly formed protein in microsomal vesicles was prepared and
examined by gel electrophoresis. In normal and starved–re-fed animals, 27% of the newly
synthesized protein was albumin. During starvation, when RNA synthesis was decreased …
Abstract
Certain qualitative aspects of protein synthesis in the livers of starved, starved–re-fed and actinomycin D-treated rats have been examined by polyacrylamide-gel electrophoresis. Animals were exposed to a mixture of 14 C-labelled acids for 18–20min. and killed, and an ultrasonic extract of newly formed protein in microsomal vesicles was prepared and examined by gel electrophoresis. In normal and starved–re-fed animals, 27% of the newly synthesized protein was albumin. During starvation, when RNA synthesis was decreased, the percentage of newly formed protein as albumin rose. After actinomycin D treatment of starved–re-fed rats, when only stable messenger RNA persisted in the cytoplasm, albumin synthesis increased to 63% of the total. This finding suggested that albumin was the primary protein synthesized on stable messenger RNA.
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