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Physiology of rat-liver polysomes. Protein synthesis by stable polysomes
Wilson, S H ; Hill, H Z ; Hoagland, M B
Biochemical Journal, 1967-05, Vol.103 (2), p.567-572
[Periódico revisado por pares]
England
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Título:
Physiology of rat-liver polysomes. Protein synthesis by stable polysomes
Autor:
Wilson, S H
;
Hill, H Z
;
Hoagland, M B
Assuntos:
Albumins - biosynthesis
;
Animals
;
Carbon Isotopes
;
Dactinomycin - pharmacology
;
Diet
;
Electrophoresis
;
Female
;
Immunodiffusion
;
Injections, Intraperitoneal
;
Liver - metabolism
;
Microsomes - analysis
;
Protein Biosynthesis
;
Rats
;
Ribosomes - metabolism
;
RNA, Messenger
;
Starvation
;
Ultrasonics
É parte de:
Biochemical Journal, 1967-05, Vol.103 (2), p.567-572
Notas:
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição:
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.
Editor:
England
Idioma:
Inglês
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