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A Rapid Method for Purification of Myelin Basic Protein
Author(s) -
Bellini Tiziana,
Rippa Mario,
Matteuzzi Maurizio,
Dallocchio Franco
Publication year - 1986
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.1471-4159.1986.tb01788.x
Subject(s) - myelin , myelin basic protein , chromatography , white matter , chemistry , protease , protein purification , homogeneous , extraction (chemistry) , myelin sheath , biochemistry , organic solvent , enzyme , biology , chemical engineering , central nervous system , medicine , thermodynamics , physics , radiology , neuroscience , magnetic resonance imaging , engineering
A rapid procedure for purification of myelin basic protein has been developed. White matter is delipidated with 2‐butanol, and the residue is extracted at pH 7.5 and 8.5. Myelin basic protein is solubilized by extraction in acetate buffer, pH 4.5. The entire procedure requires less than 4 h, and gives homogeneous protein essentially free of protease activity. This procedure can be scaled down to process milligram amounts of white matter; thus it can be very useful for purification of myelin basic protein from very limited amounts of human white matter obtained during surgery.