Purification of the human alpha2 Isoform of Na,K-ATPase expressed in Pichia pastoris. Stabilization by lipids and FXYD1.

@article{Lifshitz2007PurificationOT,
  title={Purification of the human alpha2 Isoform of Na,K-ATPase expressed in Pichia pastoris. Stabilization by lipids and FXYD1.},
  author={Yael R. Lifshitz and Ekaterina Petrovich and Haim Haviv and Rivka Goldshleger and Daniel M. Tal and Haim Garty and Steven J D Karlish},
  journal={Biochemistry},
  year={2007},
  volume={46 51},
  pages={
          14937-50
        }
}
Human alpha1 and alpha2 isoforms of Na,K-ATPase have been expressed with porcine 10*Histidine-tagged beta1 subunit in Pichia pastoris. Methanol-induced expression of alpha2 is optimal at 20 degrees C, whereas at 25 degrees C, which is optimal for expression of alpha1, alpha2 is not expressed. Detergent-soluble alpha2beta1 and alpha1beta1 complexes have been purified in a stable and functional state. alpha2beta1 shows a somewhat lower Na,K-ATPase activity and higher K0.5K compared to alpha1beta1… CONTINUE READING
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