埃德曼退化
微管蛋白
残留物(化学)
部分
生物化学
氨基酸
微管
化学
细胞生物学
生物
肽序列
立体化学
基因
作者
Bernard Eddé,Jean Rossier,Jean‐Pierre Le Caër,E. Desbruyères,François Gros,Philippe Denoulet
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:1990-01-05
卷期号:247 (4938): 83-85
被引量:508
标识
DOI:10.1126/science.1967194
摘要
The high degree of tubulin heterogeneity in neurons is controlled mainly at the posttranslational level. Several variants of alpha-tubulin can be posttranslationally labeled after incubation of cells with [3H]acetate or [3H]glutamate. Peptides carrying the radioactive moiety were purified by high-performance liquid chromatography. Amino acid analysis, Edman degradation sequencing, and mass spectrometric analysis of these peptides led to the characterization of a posttranslational modification consisting of the successive addition of glutamyl units on the gamma-carboxyl group of a glutamate residue (Glu445). This modification, localized within a region of alpha-tubulin that is important in the interactions of tubulin with microtubule-associated proteins and calcium, could play a role in regulating microtubule dynamics.
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