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METHYLATION OF MYELIN BASIC PROTEIN BY ENZYMES FROM RAT BRAIN
Author(s) -
Jones Gwyneth M.,
Carnegie P. R.
Publication year - 1974
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.1471-4159.1974.tb12222.x
Subject(s) - methyltransferase , methylation , myelin basic protein , biochemistry , enzyme , myelin , methionine , transferase , histone , arginine , protein arginine methyltransferase 5 , biology , protein methylation , cytoplasm , chemistry , microbiology and biotechnology , amino acid , endocrinology , central nervous system , gene
— In rat brain Methylase l activity ( S ‐adenosyl‐ l ‐methionine: protein‐arginine methyl‐transferase) is found predominantly in the cytoplasmic fraction, and it appears that several enzymes contribute to this activity. No evidence for the existence of two enzymes specific for the methylation of histone and myelin basic protein was found. The specific activity of Methylase I did not increase at the period of rapid synthesis of myelin basic proteins. Methylase I activity was strongly inhibited by S ‐adenosyl‐ l ‐homocysteine.