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  • Title: A glycolytic enzyme binding domain on tubulin.
    Author: Volker KW, Knull Hr.
    Journal: Arch Biochem Biophys; 1997 Feb 15; 338(2):237-43. PubMed ID: 9028878.
    Abstract:
    Cleavage of tubulin at tryptophan residues yielded several peptides, one of which strongly interacted with aldolase as determined by inhibition of aldolase activity. This peptide was identified as the C-terminal, residues 408-451, of the alpha-subunit of tubulin. Peptides with identical sequences to the C-terminal regions of the alpha- and beta-subunits of tubulin were synthesized to further characterize interactions with glycolytic enzymes. A 43-amino-acid C-terminal peptide from alpha-tubulin (residues 409-451) was found to have binding properties similar to those of native tubulin and was designated the tubulin glycolytic enzyme binding domain (T-GEBD-43mer).
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