The microtubule-associated protein tau has been isolated and purified from both white and grey brain matter. Tau isoforms were fractionated, based on their different phosphate contents, by iron-chelating affinity chromatography. Differences were observed in the proportions of phosphorylated isoforms of tau protein (containing four tubulin-binding motifs) present in white and grey matter. In white matter, isoforms containing four tubulin-binding motifs are mainly present in a phosphorylated form. Thus there appears to be a correlation between the modification, by phosphorylation, of some sites in the tau molecule and the subcellular localization (axonal or somatodendritic compartments) of the modified isoforms.
Research Article| December 01 1993
Differential distribution in white and grey matter of tau phosphoisoforms containing four tubulin-binding motifs
J G de Ancos;
Biochem J (1993) 296 (2): 351–354.
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J G de Ancos, J Avila; Differential distribution in white and grey matter of tau phosphoisoforms containing four tubulin-binding motifs. Biochem J 1 December 1993; 296 (2): 351–354. doi: https://doi.org/10.1042/bj2960351
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