ISSN:
1573-4943
Keywords:
Sea urchin
;
axoneme
;
tubulin
;
posttranslational modifications
;
polyglycylation
;
polyglutamylation
;
edman degradation
;
mass spectrometry
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract 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 α-tubulin.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1026336722124
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