PROTEIN METHYLATION IN RAT BRAIN IN VITRO

Abstract— Protein-methylation activity in various organs of the rat was studied with S-adenosyl-L-[methyl-¹⁴C]methionine ([methyl-¹⁴C](SAM) as methyl donor. Activity of the enzyme was highest in brain and lowest in liver. Histones comprised approximately 20 per cent of the total radioactivity incorporated, and lysine-rich histone was the most active. Analysis of amino acids of the methylated proteins of rat brain showed arginine to be the amino acid most extensively methylated, but some methylation occurred in lysine residues. An additional [methyl-¹⁴C]-labelled amino acid was found near histidine on the amino acid column chromatogram.