Purification and characterisation of tubulin from the parasitic nematode, Ascaridia galli.

We have developed a method for the purification of tubulin from a parasitic nematode using DEAE-Sephadex column chromatography and temperature-dependent assembly. The resulting microtubules were morphologically similar to those obtained from mammalian brain. The nematode tubulin showed similar properties to mammalian tubulin on one and two dimensional polyacrylamide gels, although certain electrophoretic conditions revealed a slight difference in the alpha-tubulins from mammals and nematodes. This was confirmed by limited proteolytic peptide mapping. The beta subunit of nematode tubulin appeared almost identical to that of mammals. Peptide maps of these tubulins were also compared with those of eukaryotic micro-organisms and these results interpreted in terms of the evolution of the tubulin polypeptides and the sensitivity of helminths to antimicrotubular agents.