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METHYLASES OF MYELIN BASIC PROTEIN AND HISTONE IN RAT BRAIN
Author(s) -
Miyake M.
Publication year - 1975
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.1471-4159.1975.tb03655.x
Subject(s) - histone , biochemistry , myelin basic protein , myelin , biology , enzyme , methylation , cell , nuclear protein , microbiology and biotechnology , endocrinology , dna , central nervous system , gene , transcription factor
—The two enzymes methylating myelin basic protein and histone were purified 170‐ and 250‐fold respectively from the cell sap fraction of rat brain. These enzymes methylated only arginine residues of the two proteins. The enzyme activities were present in all organs tested. Testis has the highest, brain a moderate and liver the lowest activity. Most of the activities were present in the cell sap fraction in brain, liver and testis. Methylation of myelin basic protein and histone was examined in both the cell sap and solubilized nuclear fraction of rat brain during life span after birth. The myelin basic protein methylating activity in the cell sap fraction increased during myelination. Histone methylase from the nuclear fraction was highest at birth and dropped rapidly thereafter. The other activities remained unchanged. The natural occurrence of N G ‐mono‐ and N G , N G ‐dimethylarginine residues in histones prepared from rabbit liver was demonstrated.