The alpha-tubulin of the growth cone is predominantly in the tyrosinated form.

Growth cone cytoskeletons were prepared by detergent extraction of growth cones isolated from neonatal rat forebrain by the method of Gordon-Weeks and Lockerbie (Neuroscience, 13 (1984) 119-136). SDS-PAGE analysis of growth cone cytoskeletons revealed the presence of several major bands, identified by their mobility as actin (43 kDa Mr), myosin heavy chain (195 kDa Mr), spectrin (235 and 240 kDa Mr), and tubulin (51-54 kDa Mr). The identity of these proteins was confirmed by immunoblot analysis using specific antibodies to these proteins which further revealed that the predominant form of alpha-tubulin in the growth cone cytoskeleton and in the soluble pool of tubulin is tyrosinated at the C-terminal.