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Deacylation of myelin proteolipid protein in organic solvents

✍ Scribed by O. A. Bizzozero; F. Dominguez; J. M. Pasquini; E. F. Soto

Publisher: John Wiley and Sons
Year: 1985
Tongue: English
Weight: 456 KB
Volume: 14
Category: Article
ISSN: 0360-4012
DOI: 10.1002/jnr.490140205

No coin nor oath required. For personal study only.

✦ Synopsis

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.

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