Comparison of the properties of tubulin from Nippostrongylus brasiliensis with mammalian brain tubulin.
Tubulin was estimated to account for 16.3% and 0.25% of protein in rat brain and Nippostrongylus brasiliensis supernatants, respectively. Tubulin from N. brasiliensis and rat brain have been partially purified using polylysine agarose chromatography and high performance liquid chromatography on a gel permeation column. Western blots with alpha- and beta-tubulin monoclonal antibodies confirmed the presence of tubulin in different fractions. The mobility of N. brasiliensis tubulin on sodium dodecyl sulfate-polyacrylamide gel electrophoresis was similar to that of rat brain tubulin. The isoelectric range for N. brasiliensis alpha- and beta-tubulin isoforms was pH 5.4-4.8 and pH 4.8-4.7, respectively. However, for rat brain the corresponding ranges were pH 5.4-4.9 and pH 5.0-4.6, respectively. Western blots with anti-tubulin monoclonal antibodies revealed 8 isoforms of alpha-tubulin and 3 isoforms of beta-tubulin for N. brasiliensis and 14-15 and 7-8 isoforms for rat brain alpha- and beta-tubulins, respectively. Different peptide maps were obtained for N. brasiliensis tubulin compared with rat brain tubulin.
Tang
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Institute of Parasitology of McGill University, Macdonald College, Ste-Anne de Bellevue, Quebec, Canada.
Prichard
R K
RK
D000818:Animals; D001923:Brain Chemistry; D002847:Chromatography, Agarose; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D007118:Immunoassay; D007525:Isoelectric Focusing; D009559:Nippostrongylus / Q000032:analysis*; D010449:Peptide Mapping; D051381:Rats; D011919:Rats, Inbred Strains; D014404:Tubulin / Q000032:analysis*
D014404:Tubulin