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Purification of Individual Subunits from the Epithelial Sodium Channel (ENaC)

The Epithelial Sodium Channel (ENaC) is vital in maintaining a homeostatic range of sodium concentration in vertebrates. A disturbance in the normal concentration of sodium inside and outside of the cell can be lethal to the cell and the organism. Studies examining this channel have concluded that at least three homologous but distinct subunits α, β, and γ compose the functional channel. These subunits work synergistically to control the Na+ travel across epithelia; however, specific subunit‐subunit interactions remain to be determined. In an effort to map the interactions of the functional channel, we have developed a purification scheme for isolating recombinant channel subunits and/or complexes. The initial purification step involves affinity purification using an engineered histidine tail on the alpha subunit. While subsequent purification of the alpha subunit involves cation exchange chromatography using a CM‐cellulose, beta and gamma subunits were purified using DEAE anion exchange chromatography. Large scale purifications are currently being performed in order to examine subunit interactions using mass spectrometry techniques.