[Identification of transcortin-synthesizing polyribosomes in the rat liver].
Transcortin biosynthesis in rats has been examined using liver slices technique. The incorporation of [14C]-labelled amino acids into the anti-transcortin-precipitable material of liver slices has been measured and compared with that of serum transcortin. It was shown that liver synthesized transcortin with an apparent molecular weight of 66 kDa on SDS-electrophoresis which co-migrated with authentic rat serum transcortin. In order to determine an intracellular distribution of transcortin-synthesizing polyribosomes, the binding character of [125J] anti-transcortin-IgG to free and membrane-bound rat liver polyribosomes has been studied. It was shown that after incubation of [125J] anti-transcortin-IgG with liver membrane-bound polyribosomes, the radioactivity was associated with the discrete polyribosome fraction in the heavy polyribosome region. In similar experiments the radioactivity of [125J] anti-transcortin-IgG bound to free polyribosomes was distributed throughout the polyribosome region.
Krauialis
K I
KI
Diashrius
A P
AP
D000818:Animals; D002499:Centrifugation, Density Gradient; D004591:Electrophoresis, Polyacrylamide Gel; D008099:Liver / Q000378:metabolism* / Q000648:ultrastructure; D008297:Male; D010452:Peptide Biosynthesis; D011132:Polyribosomes / Q000378:metabolism*; D051381:Rats; D014156:Transcortin / Q000096:biosynthesis*
D014156:Transcortin
Identifikatsiia transkortinsinteziruiushchikh poliribosom pecheni krys.