Physics
Scientific paper
Oct 1975
adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1975natur.257..496w&link_type=abstract
Nature, Volume 257, Issue 5526, pp. 496-498 (1975).
Physics
3
Scientific paper
TUBULIN, the primary protein of microtubules1,2, has been identified as a major soluble protein in isolated synaptosomes3,4. Indirect evidence for the presence of tubulin in the synaptosomal plasma membranes themselves has been accumulating for some time. Colchicine-binding activity, used as an assay for the presence of tubulin1,2, has been found in synaptosomal plasma membranes5-7. These membranes, prepared by several different techniques, all show a prominent protein band of apparent molecular weight 52,000-53,000 when solubilised and electrophoresed in sodium dodecyl sulphate-polyacrylamide gel systems8-12 such gel techniques applied to well characterised microtubule preparations yield molecular weights for tubulin which have been reported to range from 52,000 to 56,000 (refs 1 and 2), the precise value depending on the particular electrophoretic system used. Sequential solubilisation of synaptosomal plasma membranes with Triton X-1000 and N-lauroyl sarcosinate yields isolated postsynaptic densities13 whose major protein has a molecular weight of 53,000 (ref. 14), and similarly digestion of the synaptosomal lipid unit membrane by sodium deoxycholate results in isolated postsynaptic junctional lattices15 with a major protein of approximate molecular weight 53,000 (ref. 12). We report here the identification of tubulin in the postsynaptic junctional lattices of rat forebrain both by two-dimensional electrophoresis of 125I-labelled tryptic peptides and by electron microscope immunohistochemistry.
Matus Andrew I.
Walters Bradford B.
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