Synthesis of actin-like protein in rat liver mitochondria

Autor:	A N, Stozharov
Rok vydání:	1986
Předmět:	Male Cytoplasm Protein Biosynthesis Animals Electrophoresis Polyacrylamide Gel Mitochondria Liver Cycloheximide In Vitro Techniques Actins Chromatography Affinity Rats
Zdroj:	General physiology and biophysics. 5(3)
ISSN:	0231-5882
Popis:	Isolated rat liver mitochondria failed to exhibit in vitro incorporation of [14C]-amino acids into actin-like protein. The use of a pulse-labelling technique demonstrated the appearance of [14C]-actin-like protein in the mitochondria of control, cycloheximide-free rats. The actin-like protein was identified by the method of affinity binding on DNAse1-sepharose and by electrophoresis on polyacrylamide gel with sodium dodecyl sulphate. It was shown that mitochondrial actin-like protein is not included among the nine polypeptides synthesized in mitochondria during cycloheximide-induced blockade of cytoplasmic protein synthesis. It was shown that actin-like protein was not desorbed from mitochondria by repeated washing with isotonic sucrose-mannitol medium. The results obtained indicate that the actin-like protein is biosynthesised in the cytoplasmic compartment.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::74b34b1b67d6d3cd771ca6287a705a09 https://pubmed.ncbi.nlm.nih.gov/3758662 Zobrazit plný text záznamu