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- W1992617653 abstract "α and β tubulin genes were cloned from the Capsicum annuum leaves using rapid amplification of cDNA ends (RACE)-PCR. Nucleotide sequence analysis revealed that 1,353 bp Capsicum annuum α⁄β-tubulin (CAnm α⁄β-TUB) encodes a protein of 450 amino acids (aa) each. The recombinant α⁄β tubulin was overexpressed mainly as an inclusion body in Escherichia coli BL21 (DE3), upon induction with 0.2 mm isopropyl-β-d-thiogalactopyranoside (IPTG), and its content was as high as 50% of the total protein content. Effective fusion protein purification and refolding are described. The average yields of α and β tubulin were 2.0 and 1.3 mg/l of culture respectively. The apparent molecular weight of each tubulin was estimated to be 55 kDa by SDS-polyacrylamide gel electrophoresis (PAGE). The tubulin monomers were found to be assembly competent using a standard dimerization assay, and also retained antigenicity with anti-His/T7 antibodies. The purified tubulins were polymerized to microtubule-like structures in the presence of 2 mm guanosine 5′-triphosphate (GTP)." @default.
- W1992617653 created "2016-06-24" @default.
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- W1992617653 date "2008-04-23" @default.
- W1992617653 modified "2023-09-24" @default.
- W1992617653 title "Cloning, Purification, and Polymerization ofCapsicum annuumRecombinant α and β Tubulin" @default.
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- W1992617653 doi "https://doi.org/10.1271/bbb.70794" @default.
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