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CHARACTERIZATION OF MULTIPLE FORMS OF BRAIN TUBULIN SUBUNITS
Author(s) -
Marotta Charles A.,
Harris Jame L.,
Gilbert Jeffrey M.
Publication year - 1978
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.1471-4159.1978.tb10475.x
Subject(s) - tubulin , isoelectric focusing , urea , sodium dodecyl sulfate , isoelectric point , chromatography , chemistry , protein subunit , biochemistry , acrylamide , ammonium sulfate precipitation , gel electrophoresis , biology , microtubule , monomer , size exclusion chromatography , microbiology and biotechnology , enzyme , organic chemistry , gene , polymer
— Microtubular protein was isolated from rat forebrain by biochemical purification (ammonium sulfate precipitation followed by DEAE cellulose chromatography) or by two cycles of aggregation‐disaggregation. The protein subunit structure was examined on two‐dimensional electrophoretograms: first dimension, urea isoelectric focusing gel; second dimension, sodium dodecyl sulfate exponential acrylamide slab gel. Two forms of α tubulin were separated in the second dimension on the basis of different rates of migration (α and α 2 ). Each of these species was further separated into at least three forms with different isoelectric points. β Tubulin was separated into a minor species (BI) and a major species β 2 ). Multiple subunits were observed using protein from either purification method and in a two‐dimensional electrophoretogram of total supernatant proteins from rat brain. Separation and visualization of multiple forms of α and β tubulin is consistent with reports that provide evidence for post‐translational modification of these proteins.