Isolation of the sodium-dependent d-glucose transport protein from brush-border membranes |
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Authors: | P Malathi H Preiser |
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Institution: | Department of Physiology and Biophysics, University of Medicine and Dentistry of New Jersey, Rutgers Medical School, Piscataway, NJ 08854 U.S.A. |
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Abstract: | Rabbit kidney brush-border membrane vesicles were exposed to bacterial protease which cleaves off a large number of externally oriented proteins. Na+-dependent d-glucose transport is left intact in the protease-treated vesicles. The protease-treated membrane was solubilized with deoxycholate and the deoxycholate-extracted proteins were further resolved by passage through Con A-Sepharose columns. Sodium-dependent d-glucose activity was found to reside in a fraction containing a single protein band of Mr ? 165000 which is apparently a dimer of Mr ? 85 000. When reconstituted and tested for transport, this protein showed Na+-dependent, stereo-specific and phlorizin-inhibitable glucose transport. Transport activity is completely recovered and is 20-fold increased in specific activity. A similar isolate was obtained from rabbit small intestinal brush-border membranes and kidneys from several other species of animals. |
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Keywords: | Glucose transport Phlorizin inhibition Brush-border membrane Membrane reconstitution (Rabbit kidney intestine) Hepes |
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