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PROTEIN METHYLATION BY CEREBRAL TISSUE
Author(s) -
Miyake M.,
Kakimoto Y.
Publication year - 1973
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1973.tb00046.x
Subject(s) - lysine , methylation , arginine , protein methylation , biochemistry , enzyme , methionine , chemistry , methyltransferase , biology , amino acid , dna
— Transfer of the methyl group of S ‐adenosyl [Me‐ 14 C]methionine into cerebral proteins, an encephalitogenic protein and histones was studied using extracts of bovine and rat brains. The brain extract contains multiple substrate proteins and their lysine and arginine residues were methylated to form N e ‐mono‐, ‐di‐ and ‐trimethyl‐lysine and N G ‐mono‐, N G , N G ‐ and N G ,N G ‐dimethylarginine residues respectively, at different rates. The enzyme which catalyses the methylation of arginine residues was differentiated by ammonium sulphate fractionation from that methylating lysine residues. Methylation of arginine and lysine residues of proteins was stepwise in general, from mono‐ to dimethyl‐arginine and from mono‐ to di‐ and trimethyl‐lysines. Two different enzymes which methylate histone and the encephalitogenic basic protein respectively were obtained from the cytoplasmic fraction of rat brain and their enzymic properties were examined.