Identification and drug binding capabilities of tubulin in the nematode Ascaridia galli.

Journal article

Cell extracts of Ascaridia galli bind colchicine in a manner suggesting the presence of a tubulin-like protein. Column chromatography of these extracts on DEAE-Sephadex yielded only one peak with colchicine-binding activity. Single peaks of radioactivity in this same position were obtained on chromatography of extracts prelabelled with either [3H]colchicine or [3H]parbendazole. Sodium dodecyl sulphate polyacrylamide gel electrophoresis and two dimensional gel electrophoresis of the fractions making up the peaks indicated the presence of two proteins which co-migrate with mammalian brain alpha- and beta-tubulin markers. More detailed investigation showed that the A. galli tubulin has a slightly different alpha-subunit when compared with mammalian tubulin.

Authors: Ireland, C; Clayton, L; Gutteridge, W; Pogson, C; Gull, K

• Publication status: Published
• Journal: Molecular and biochemical parasitology
• Volume: 6
• Issue: 1
• Pages: 45-53
• Publication date: 1982-07-01
• DOI: 10.1016/0166-6851(82)90052-4
• EISSN: 1872-9428
• ISSN: 0166-6851
• Language: English
• Keywords: Electrophoresis, Polyacrylamide Gel; Ascaridia; Colchicine; Tubulin; Protein Binding; Animals; Molecular Weight