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Deacylation of myelin proteolipid protein in organic solvents
Author(s) -
Bizzozero O. A.,
Dominguez F.,
Pasquini J. M.,
Soto E. F.
Publication year - 1985
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490140205
Subject(s) - chemistry , hydroxylamine , chloroform , organic solvent , myelin , covalent bond , methanol , proteolipid protein 1 , chromatography , organic chemistry , solvent , myelin proteolipid protein , biochemistry , myelin basic protein , biology , chemical engineering , neuroscience , engineering , central nervous system
A procedure has been developed for the deacylation of the hydrophobic, myelin proteolipid apoprotein using hydroxylamine in an alkaline organic solvent medium. Complete removal of covalently bound fatty acids was obtained after 4 hr of treatment. After deacylation, no changes could be detected in the electrophoretic pattern or in the number of free sulfhydryl groups. The deacylated apoprotein remains soluble in chloroform‐methanol mixtures and is suitable for further physicochemical characterization.