Volker K W, Knull H r
School of Medicine, Edwin C. James Research Facility, University of North Dakota, 501 North Columbia Road, Grand Forks, North Dakota, 58202, USA.
Arch Biochem Biophys. 1997 Feb 15;338(2):237-43. doi: 10.1006/abbi.1996.9819.
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).
微管蛋白在色氨酸残基处的裂解产生了几种肽段，其中一种通过抑制醛缩酶活性测定，与醛缩酶强烈相互作用。该肽段被鉴定为微管蛋白α亚基的C末端，即408 - 451位残基。合成了与微管蛋白α和β亚基C末端区域具有相同序列的肽段，以进一步表征与糖酵解酶的相互作用。发现来自α微管蛋白的一个43个氨基酸的C末端肽段（409 - 451位残基）具有与天然微管蛋白相似的结合特性，并被命名为微管蛋白糖酵解酶结合结构域（T - GEBD - 43mer）。
