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Purification and Chemical Characterization of a W2 Protein from Brain Myelin
Author(s) -
Reig J. A.,
Ramos J. M.,
Cozar M.,
Aguilar J. S.,
Criado M.,
Monreal J.
Publication year - 1982
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.1471-4159.1982.tb03973.x
Subject(s) - myelin , characterization (materials science) , chemistry , myelin basic protein , neuroscience , biology , nanotechnology , central nervous system , materials science
Starting from a pellet of beef brain myelin insoluble in chloroform/ methanol (2:1, vol/vol) (Wolfgram protein fraction), a pure W2 protein with apparent molecular weight of 52,000 was isolated by a simple preparative sodium dodecyl sulfate‐polyacrylamide gel electrophoresis method. A comparative chemical analysis was carried out between purified W2 and a standard tubulin. Glutamic acid and arginine were the N‐terminals detected. Similar peptide maps and amino acid composition were also found in both proteins. Immunological cross‐reactivity was detected when W2 protein was tested against antitubulin serum. These results suggest that W2 protein could have a tubulin‐like protein nature that is associated with the myelin membrane and could play a role in the myelination process.