title: A glycolytic enzyme binding domain on tubulin.
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).
authors.affiliation: School of Medicine, Edwin C. James Research Facility, University of North Dakota, 501 North Columbia Road, Grand Forks, North Dakota, 58202, USA.
authors.forename: K W
authors.initials: KW
authors.lastname: Volker
authors.forename: H r
authors.initials: Hr
authors.lastname: Knull
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001457:Anion Exchange Protein 1, Erythrocyte / Q000378:metabolism; D002417:Cattle; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D005971:Glutamates / Q000737:chemistry; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D006019:Glycolysis; D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism; D011485:Protein Binding; D011770:Pyruvate Kinase / Q000378:metabolism; D011817:Rabbits; D014364:Tryptophan / Q000737:chemistry; D014404:Tubulin / Q000378:metabolism*
chemical_list: D001457:Anion Exchange Protein 1, Erythrocyte; D005971:Glutamates; D007527:Isoenzymes; D010446:Peptide Fragments; D014404:Tubulin; D014364:Tryptophan; D007770:L-Lactate Dehydrogenase; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D011770:Pyruvate Kinase; D005634:Fructose-Bisphosphate Aldolase