1. Characterization of Capsicum annuum recombinant alpha- and beta-tubulin.
- Author
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Koo BS, Jang MH, Park H, Kalme S, Park HY, Han JW, Yeo YS, Yoon SH, Kim SJ, Lee CM, and Yoon MY
- Subjects
- Dithionitrobenzoic Acid metabolism, Indicators and Reagents pharmacology, Protein Multimerization drug effects, Protein Structure, Quaternary, Temperature, Tubulin chemistry, Capsicum, Plant Proteins chemistry, Plant Proteins metabolism, Recombinant Proteins chemistry, Recombinant Proteins metabolism, Tubulin metabolism
- Abstract
There are several conditions which might modulate polymerization to produce polymers having normal lattice structure. In the absence of 1 mM MgCl(2) the assembly was reduced by 36% in Capsicum annuum tubulin (CAnm tubulin). There was no significant difference in the final assembly formation in the presence of 5% to 10% glycerol. However, nucleation rate was slow and apparent study state was achieved lately in the presence of 10% glycerol. Taxol at 100 microM concentration increased 23% tubulin assembly. One millimolar CaCl(2), >or=1% dimethyl sulfoxide (DMSO) and physiologically low temperature reduced CAnm tubulin assembly. A value of 0.089 mg/ml was obtained as critical concentration for polymerization. Benomyl significantly reduced the number of cysteine residues accessible to 5,5'-dithiobis-(2-nitrobenzoic acid); there were 4.77 +/- 0.21 and 3.49 +/- 0.35 residues accessible per tubulin dimer in the presence of 50 and 100 microM benomyl respectively.
- Published
- 2010
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