Maltose-binding protein from the hyperthermophilic bacterium Thermotoga maritima: stability and binding properties.

@article{Wassenberg2000MaltosebindingPF,
  title={Maltose-binding protein from the hyperthermophilic bacterium Thermotoga maritima: stability and binding properties.},
  author={Deena Wassenberg and Wolfgang Liebl and R. C. A. Jaenicke},
  journal={Journal of molecular biology},
  year={2000},
  volume={295 2},
  pages={
          279-88
        }
}
Recombinant maltose-binding protein from Thermotoga maritima (TmMBP) was expressed in Escherichia coli and purified to homogeneity, applying heat incubation of the crude extract at 75 degrees C. As taken from the spectral, physicochemical and binding properties, the recombinant protein is indistinguishable from the natural protein isolated from the periplasm of Thermotoga maritima. At neutral pH, TmMBP exhibits extremely high intrinsic stability with a thermal transition >105 degrees C… CONTINUE READING
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