Výsledky vyhledávání - "Heidi Winkelbach"

Channel Active Mammalian Porin, Purified from Crude Membrane Fractions of Human B Lymphocytes and Bovine Skeletal Muscle, Reversibly Binds Adenosine Triphosphate (ATP)

Autor: Anton Karabinos, Ulrike Stadtmüller, Volker E. Lalk, Hans Sternbach, Corinna Morys-Wortmann, Heidi Winkelbach, Norbert Hilschmann, Martin Heiden, Gabriele Paetzold, Friedrich P. Thinnes, Susanne Reymann, Petra Kaufmann-Kolle, Dörte Hesse, Bodo Zimmermann, Harald Flörke

Publikováno v: Biological Chemistry Hoppe-Seyler. 375:513-520

A new aspect of mammalian porin (mammalian VDAC = mammalian voltage-dependent anion channel) is presented: channel active VDAC binds adenosine triphosphate (ATP) in the absence of Ca2+. Channel active "Porin 31HL" or "Porin 31BM", enriched from crude

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f7eb78930d9ffe40702b6dfd997a8d7
https://doi.org/10.1515/bchm3.1994.375.8.513

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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

Autor: Martin Heiden, Eduard Fleer, Ulrike Stadtmüller, Hartmut Kratzin, Friedrich P. Thinnes, Harald Flörke, Dörte Hesse, Heidi Winkelbach, Norbert Hilschmann, Anton Karabinos

Publikováno v: Biological chemistry Hoppe-Seyler. 375(5)

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'-di

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e25529ea2a28d38ad2d4a6b706b3820c
https://pubmed.ncbi.nlm.nih.gov/8074805

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