Comparison of the acetylation of proteins and nucleic acids.
The possibility of acetylation of nucleic acids was examined. Although protein is actively acetylated with [1-(14)C]acetic acid in rat liver systems in vivo and in vitro and in a frog liver system in vivo, nucleic acids are not acetylated under these conditions; nucleic acids purified from these sources are without radioactivity. Requirements for acetylation in vitro of protein in rat liver are different from those in frog liver; GSH has no effect in the rat liver system and is inhibitory in the frog liver system. Among various acetylated proteins, proteins insoluble in 0.1m-sulphuric acid have the highest radioactivity.
D000085:Acetates / Q000378:metabolism*; D000818:Animals; D001001:Anura; D002247:Carbon Isotopes; D003851:Deoxyribonucleases / Q000378:metabolism; D005978:Glutathione / Q000494:pharmacology; D066298:In Vitro Techniques; D008099:Liver / Q000378:metabolism; D009696:Nucleic Acids / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D051381:Rats; D012260:Ribonucleases / Q000378:metabolism; D012995:Solubility; D013464:Sulfuric Acids; D014357:Trypsin
D000085:Acetates; D002247:Carbon Isotopes; D009696:Nucleic Acids; D011506:Proteins; D013464:Sulfuric Acids; D003851:Deoxyribonucleases; D012260:Ribonucleases; D014357:Trypsin; D005978:Glutathione