Premium
Posttranslational Incorporation of [ 14 C]Arginine into Rat Brain Proteins. Acceptor Changes During Development
Author(s) -
Hallak Marta E.,
Barra H. S.,
Caputto R.
Publication year - 1985
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.1471-4159.1985.tb12865.x
Subject(s) - cytosol , arginine , biochemistry , chemistry , isozyme , electrophoresis , albumin , enzyme , transferase , biology , microbiology and biotechnology , amino acid
Many of the cytosolic proteins of the rat brain appear to have the capacity to incorporate l ‐[ 14 C]arginine posttranslationally. Scanning of the electrophoretic pattern of the labeled proteins showed two main radioactive peaks: peak A, found in the region of proteins of MW above 200 kD, and peak B, found in the region of 33 kD. The ratio of peaks A/B tends to decrease with the age of the rats. Another zone of radioactivity has an apparent MW similar to that of albumin (approximately 66 kD). No differences were found between the effects of ionic strength and of inhibitors on the arginyl transferase of brain and those described for the transferases of other organs.