Abstract
Myelin basic protein has been isolated from bovine central-nervous-system myelin by four methods, none of which exposes the protein to acid. After purification the inositol content of both hydrolysed and unhydrolysed protein was quantified by g.c.-m.s. Basic protein prepared by all methods contained less than 4 mol % of inositol. It is concluded, contrary to a previous proposal, that covalent binding to phosphoinositides does not represent a general mechanism for attachment of this cytoplasmically-oriented protein to its membrane.
| Original language | English |
|---|---|
| Pages (from-to) | 285-288 |
| Number of pages | 4 |
| Journal | Biochemical Journal |
| Volume | 248 |
| Issue number | 1 |
| Publication status | Published - 15 Nov 1987 |