Výsledky vyhledávání - "Harald Flörke"

Studies on Human Porin

Autor: Friedrich P. Thinnes, Susanne Reymann, Dörte Hesse, G. Paetzold, C. Moryswortmann, Götz Walter, H. Winkelbach, Harald Flörke, B. Zimmermann, Ulrike Stadtmüller, N. Hilschmann

Publikováno v: Biochemical Medicine and Metabolic Biology. 52:120-127

Eight mouse monoclonal antibodies directed against the acetylated N-terminal part of the type 1 human VDAC Porin 31HL clearly discriminate type 1 and type 2 mammalian porin channels. This is shown by comparing synthetic N-terminal peptides of either

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2006afa84a541bc011f2f7b550af1f57
https://doi.org/10.1006/bmmb.1994.1042

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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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Studies on human porin: XIII. The type-1 VDAC 'porin 31HL' biotinylated at the plasmalemma of trypan blue excluding human B lymphocytes

Autor: Klaus P. Hellmann, Hilde Götz, Christian Jakob, Norbert Hilschmann, Harald Flörke, Thea Hellmann, Susanne Reymann, Friedrich P. Thinnes

Publikováno v: FEBS letters. 368(1)

In 1989, we demonstrated for the first time the expression of the VDAC ‘Porin 31HL’ in the plasmalemma of human B lymphocytes, then giving first evidence of a multi-topological expression of VDAC. Meanwhile, data from this and other laboratories

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d44c6a5773911bed726738ed0534f3d
https://pubmed.ncbi.nlm.nih.gov/7542206

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Further evidence for multitopological localization of mammalian porin (VDAC) in the plasmalemma forming part of a chloride channel complex affected in cystic fibrosis and encephalomyopathy

Autor: I. Pardowitz, Friedrich P. Thinnes, Susanne Reymann, Ulrike Stadtmüller, Harald Flörke, Martin Heiden, P. Steinacker, C. Jakob, V.E. Lalk

Publikováno v: Biochemical and molecular medicine. 54(2)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8fc42b37f7acaf5d7474de3afbebbbe
https://pubmed.ncbi.nlm.nih.gov/8581362

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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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