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ECB-ART-36692
J Protein Chem 1997 Jul 01;165:403-7. doi: 10.1023/a:1026336722124.
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Posttranslational modifications of axonemal tubulin.

Mary J , Redeker V , Le Caer JP , Rossier J , Schmitter JM .


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Axonemal tubulin exhibits a high degree of heterogeneity mostly due to several posttranslational modifications (PTM). The aim of this work was to chemically characterize the different PTM occurring in the C-terminal tail of axonemal tubulin purified from sea urchin, Paracentrotus lividus, spermatozoa. After its purification, tubulin was enzymatically cleaved. The C-terminal peptides were chromatographically isolated, first by anion exchange and then by reverse-phase HPLC. Peptides were characterized by their sequence, determined by Edman degradation, and by their mass, determined by MALDI-TOF/MS. The two major conclusions are that the majority of the isolated C-terminal peptides were unmodified and that polyglycylation and polyglutamylation can occur simultaneously on one molecule of alpha-tubulin.

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Genes referenced: dnah3 LOC100887844 tubgcp2

References [+] :
Barra, A soluble preparation from rat brain that incorporates into its own proteins ( 14 C)arginine by a ribonuclease-sensitive system and ( 14 C)tyrosine by a ribonuclease-insensitive system. 1973, Pubmed