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Blumenthal A, Kahn K, Beja O, et al. Purification and Characterization of the Voltage-Dependent Anion-Selective Channel Protein from Wheat Mitochondrial Membranes. Plant Physiol. 1993;101(2):579-587doi: 10.1104/pp.101.2.579.
Blumenthal, A., Kahn, K., Beja, O., Galun, E., Colombini, M., & Breiman, A. (1993). Purification and Characterization of the Voltage-Dependent Anion-Selective Channel Protein from Wheat Mitochondrial Membranes. Plant physiology, 101(2), 579-587. https://doi.org/10.1104/pp.101.2.579
Blumenthal, A., et al. "Purification and Characterization of the Voltage-Dependent Anion-Selective Channel Protein from Wheat Mitochondrial Membranes." Plant physiology vol. 101,2 (1993): 579-587. doi: https://doi.org/10.1104/pp.101.2.579
Blumenthal A, Kahn K, Beja O, Galun E, Colombini M, Breiman A. Purification and Characterization of the Voltage-Dependent Anion-Selective Channel Protein from Wheat Mitochondrial Membranes. Plant Physiol. 1993 Feb;101(2):579-587. doi: 10.1104/pp.101.2.579. PMID: 12231713; PMCID: PMC160607.
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Plant Physiol. 1993 Feb;101(2):579-587. doi: 10.1104/pp.101.2.579.

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

Plant physiology

A. Blumenthal, K. Kahn, O. Beja, E. Galun, M. Colombini, A. Breiman

Affiliations

  1. Department of Plant Genetics (A.B., E.G.) and Department of Membrane Research and Biophysics (O.B.), The Weizmann Institute of Science, Rehovot 76100, Israel.

PMID: 12231713 PMCID: PMC160607 DOI: 10.1104/pp.101.2.579

Abstract

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 charged matrix. Subsequently, this protein was separated from the remaining polypeptides by a preferential elution from a hydroxylapatite/celite mixed column. Reconstituted liposomes containing this protein were characterized as being permeable to 8-amino-naphthalene 1,3,6-trisulfonic acid disodium salt (Mr 445) but non-permeable to dextran fluorescein (Mr 40,000). Additionally, MmP29 was inserted into planar phospholipid membranes, and anion-selective, voltage-dependent channels were demonstrated. All of the MmP29 properties mentioned highly resemble voltagedependent, anion-selective channel (VDAC) proteins, suggesting that MmP29 is the mitochondrial outer membrane VDAC protein of wheat.

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