In vivo phosphorylation of two myelin basic proteins of developing rabbit brain.

Examination of 15-day-old rabbit brain myelin proteins by sodium dodecyl sulfate-slab gel electrophoresis revealed the presence of a basic protein with a molecular weight of 21,000 (21K protein) which was not previously reported in this species. This protein exhibited characteristic bluish green color with amido black and gave an amino acid composition strikingly similar to large basic protein (LBP). It formed a line of identity with LBP when diffused against antiserum to chicken brain basic protein. The concentration of LBP (18.9 micrograms/mg of dry myelin) is 6-fold greater than that of the 21K protein(3.31 micrograms/mg of dry myelin) in rabbit brain myelin. After the intracerebral injection of [32P]orthophosphoric acid, both LBP and 21K protein were found to be phosphorylated. [32P]Phosphate in the purified preparations of these proteins was covalently linked by phosphoester bonds to serine and threonine residues. The specific radioactivity of the 21K protein (84,693 cpm/mg of protein) was not significantly higher than LBP (69,797 cpm/mg of protein).