Characterization of a purified co-transporting protein.
1. A protein of mol weight 280,000 D was isolated and purified by means of a furosemide affinity gel. 2. Binding of 3H-bumetanide suggests that the protein is identical to the Na-K-2Cl co-transporter. 3. If the protein was reconstituted into a planer lipid bilayer, a Cl- -channel of 12 pS and a K+-channel of about 130 pS was observed. 4. Whether these channel activities represent a co-purification of channel proteins or whether the channel activity originates from the purified and reconstituted co-transporting protein itself was discussed.
D000818:Animals; D001692:Biological Transport; D002352:Carrier Proteins / Q000302:isolation & purification*; D002417:Cattle; D018118:Chloride Channels; D002712:Chlorides / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D005665:Furosemide; D007672:Kidney Cortex / Q000502:physiology; D008565:Membrane Proteins / Q000302:isolation & purification*; D015221:Potassium Channels / Q000502:physiology*
D002352:Carrier Proteins; D018118:Chloride Channels; D002712:Chlorides; D008565:Membrane Proteins; D015221:Potassium Channels; D005665:Furosemide