Distribution of tyrosinated and detyrosinated alpha-tubulin revealed by mouse anti-peptide polyclonal antibodies.

Mouse anti-peptide antibodies that specifically react (in competitive ELISA and immunoblotting) with the corresponding C-terminal hepta- and octapeptides of alpha-tubulin differing in the terminal tyrosine and that hence recognize the post-translationally modified forms of alpha-tubulin are described. At the light microscopic level tyrosinated tubulin was demonstrated practically in all structures containing microtubules with the exception of the flagella of the spermatozoa of several species. The presence of detyrosinated Glu tubulin was very limited; occasional interphase microtubules, midbody and flagella of the spermatozoa only exhibited the positive reaction. The results compared to the recently published findings indicate that the different arrangement of microtubules assembled mostly of Glu tubulin can be distinguished by polyclonal antibodies against detyrosinated tubulin.