Channel active mammalian porin, purified from crude membrane fractions of human B lymphocytes or bovine skeletal muscle, reversibly binds the stilbene-disulfonate group of the chloride channel blocker DIDS.

@article{Thinnes1994ChannelAM,
  title={Channel active mammalian porin, purified from crude membrane fractions of human B lymphocytes or bovine skeletal muscle, reversibly binds the stilbene-disulfonate group of the chloride channel blocker DIDS.},
  author={Friedrich P. Thinnes and Holger Fl{\"o}rke and H Winkelbach and Ulrich Stadtm{\"u}ller and M Heiden and Anton Karabinos and Doerte Hesse and Hartmut D. Kratzin and E Fleer and Norbert Hilschmann},
  journal={Biological chemistry Hoppe-Seyler},
  year={1994},
  volume={375 5},
  pages={315-22}
}
Two new aspects of mammalian porin are presented. First, by affinity chromatography we show that channel active human or bovine porin reversibly bind the stilbene-disulfonate group of the chloride channel blocker 4,4'-diisothiocyanatostilbene-2,2'-disulfonate (DIDS). The procedure is suitable for further purification of porin after enrichment by ion exchange chromatography and shows a yield of 24.3%. The data support our recent proposal that VDAC forms part of the ORDIC channel complex which is… CONTINUE READING

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