Functional analysis of a disulfide bond in the cardiac Na(+)-Ca(2+) exchanger.

@article{SantacruzToloza2000FunctionalAO,
  title={Functional analysis of a disulfide bond in the cardiac Na(+)-Ca(2+) exchanger.},
  author={L Santacruz-Toloza and Michela Ottolia and Debora A. Nicoll and Kenneth D. Philipson},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 1},
  pages={182-8}
}
The electrophoretic mobility of the cardiac Na(+)-Ca(2+) exchange protein is different under reducing and nonreducing conditions. This mobility shift is eliminated in a cysteine-less exchanger, suggesting that the presence or absence of an intramolecular disulfide bond alters the conformation and mobility of the exchanger. Using cysteine mutagenesis and biochemical analysis, we have identified the cysteine residues involved in the disulfide bond. Cysteine 792 in loop h of the exchanger forms a… CONTINUE READING

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