Binding of rat liver and hepatoma polyribosomes to stripped rough endoplasmic reticulum in vitro. Biological or an artifact?
Exposed thiol groups do not appear to be related to the binding of (32)P-labelled polyribosomes to stripped rough endoplasmic reticulum in vitro. Treating stripped rough endoplasmic reticulum with GSSG did not diminish binding of polyribosomes, suggesting that binding in vitro has no correlation with the inhibition of protein synthesis in vitro reported by Kosower et al. (1971). Thiol reagents, which are known to dissociate ribosomes, did not significantly decrease binding of (32)P-labelled polyribosomes to stripped rough endoplasmic reticulum. Denaturing the protein of (32)P-labelled polyribosomes or stripped rough endoplasmic reticulum of liver or hepatoma with heat, trichloroacetic acid, or HClO(4) did not alter the binding in vitro. Therefore, the practice of measuring the binding of (32)P-labelled polyribosomes to stripped rough endoplasmic reticulum in vitro (Shires et al., 1971b) is an unsuitable indicator of biological significance in the intact cell.
D000818:Animals; D001665:Binding Sites; D006528:Carcinoma, Hepatocellular; D002499:Centrifugation, Density Gradient; D004721:Endoplasmic Reticulum; D005260:Female; D066298:In Vitro Techniques; D008099:Liver; D008113:Liver Neoplasms; D010759:Phosphorus Isotopes; D011132:Polyribosomes; D011489:Protein Denaturation; D011506:Proteins / Q000032:analysis; D051381:Rats; D013438:Sulfhydryl Compounds; D013696:Temperature; D014238:Trichloroacetic Acid
D010759:Phosphorus Isotopes; D011506:Proteins; D013438:Sulfhydryl Compounds; D014238:Trichloroacetic Acid