Deacylation of myelin proteolipid protein in organic solvents.
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.
Bizzozero
O A
OA
Dominguez
F
F
Pasquini
J M
JM
Soto
E F
EF
D000215:Acylation / Q000379:methods; D000818:Animals; D001053:Apolipoproteins / Q000032:analysis; D001923:Brain Chemistry; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D005227:Fatty Acids / Q000032:analysis; D006898:Hydroxylamines / Q000494:pharmacology; D009185:Myelin Proteins / Q000032:analysis / Q000378:metabolism*; D018991:Myelin Proteolipid Protein; D051381:Rats; D012997:Solvents; D013438:Sulfhydryl Compounds / Q000032:analysis
D001053:Apolipoproteins; D005227:Fatty Acids; D006898:Hydroxylamines; D009185:Myelin Proteins; D018991:Myelin Proteolipid Protein; D012997:Solvents; D013438:Sulfhydryl Compounds