Purification and Characterization of the Voltage-Dependent Anion-Selective Channel Protein from Wheat Mitochondrial Membranes.

@article{Blumenthal1993PurificationAC,
  title={Purification and Characterization of the Voltage-Dependent Anion-Selective Channel Protein from Wheat Mitochondrial Membranes.},
  author={Antje Blumenthal and Kenneth B. Kahn and Oded B{\'e}j{\`a} and Esra Galun and Marco Colombini and Adina Breiman},
  journal={Plant physiology},
  year={1993},
  volume={101 2},
  pages={579-587}
}
An approximately 29-kD protein was purified from the membrane fraction of wheat (Triticum aestivum cv Dganit) mitochondria by the utilization of standard liquid chromatography techniques. The protein, designated MmP29 for mitochondrial membrane protein having a molecular mass of approximately 29 kD, exhibited cationic properties in a buffering solution, adjusted to pH 7.5. This positive charge enabled its passage through a diethylaminoethyl column, without interaction with the positively… CONTINUE READING

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