Výsledky vyhledávání - "Sigrid Lepke"

Mediation of inorganic anion transport by the hydrophobic domain of mouse erythroid band 3 protein expressed in oocytes of Xenopus laevis

Autor: Sigrid Lepke, Anja Becker, Hermann Passow

Publikováno v: Biochimica et Biophysica Acta (BBA) - Biomembranes. 1106:13-16

A cDNA clone of the mouse erythroid band 3 protein encoding the 556 amino acid residues of the hydrophobic domain from Thr-374 to the C-terminal Val-929 is shown by immunoprecipitation to be expressed in Xenopus oocytes. Measurements of 36Cl- efflux

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::835bf3f9cfa1e62b1f1c8034000992fd
https://doi.org/10.1016/0005-2736(92)90215-8

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The Band 3 Protein: Anion Exchanger and Anion-Proton Cotransporter

Autor: Hermann Passow, Sigrid Lepke, Joachim Heberle

Publikováno v: Red Cell Membrane Transport in Health and Disease ISBN: 9783642079207

The anion transport protein of the red blood cell membrane, the so-called band 3 protein, mediates two distinct processes: anion exchange and anion-proton co-transport. The present chapter deals with the relationship between the two processes.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::bc9bd7802ca8ee652718e0117498cd60
https://doi.org/10.1007/978-3-662-05181-8_10

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Inhibition of mouse erythroid band 3-mediated chloride transport by site-directed mutagenesis of histidine residues and its reversal by second site mutation of Lys 558, the locus of covalent H2DIDS binding

Autor: Phillip G. Wood, Heribert Appelhans, Jörg König, Doris Karbach, Hermann Passow, Sigrid Lepke, Suzanne Müller-Berger

Publikováno v: Biochemistry. 34(29)

Substitution by site-directed mutagenesis of any one of the histidine residues H721, H837, and H852 by glutamine, or of H752 by serine, inhibits Cl- flux mediated by band 3 expressed in Xenopus oocytes. Mutation of Lys 558 (K558N), the site of covale

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::035677323be84ba11f6f462bea62477e
https://pubmed.ncbi.nlm.nih.gov/7626600

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Exploration of the functional significance of the stilbene disulfonate binding site in mouse band 3 by site-directed mutagenesis

Autor: Phillip G. Wood, Hermann Passow, Mika Sovak, Hannelore Müller, Sigrid Lepke

Publikováno v: Biophysical journal. 62(1)

In 1985, it was shown that microinjection into Xenopus oocytes of mRNA prepared from the spleens of anemic mice leads to biosynthesis of band 3 protein (as shown by immunoprecipitation) and induction of a CIflux, which is not normally seen in the ooc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa37820cb4ed5574591159178282488b
https://pubmed.ncbi.nlm.nih.gov/1600108

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pH-dependence of inhibition by H2DIDS of mouse erythroid band 3-mediated Cl- transport in Xenopus oocytes. The effect of oligonucleotide-directed replacement of Lys-558 by an Asn residue

Autor: Daniel Kietz, Detlef Bartel, Hermann Passow, Sigrid Lepke

Publikováno v: Biochimica et biophysica acta. 1064(1)

The rapid reversible inhibition of band 3-mediated inorganic anion transport by 4,4′-diisothiocyanodihydrostilbene-2,2′-disulfonate (H 2 DIDS) turns slowly into irreversible inhibition. This is due to covalent bond formation of the two isothiocya

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c7df863ecf406f77ade5522d8ab70bf
https://pubmed.ncbi.nlm.nih.gov/1902748

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A study of the relationship between inhibition of anion exchange and binding to the red blood cell membrane of 4,4′-diisothiocyano stilbene-2,2′-disulfonic acid (DIDS) and its dihydro derivative (H2DIDS)

Autor: Hugo Fasold, Hermann Passow, M. Pring, Sigrid Lepke

Publikováno v: The Journal of Membrane Biology. 29:147-177

DIDS (4,4'-diisothiocyano stilbene-2,2'-disulfonic acid) and H2DIDS (4,4'-diisothiocyano-1,2-diphenyl ethane-2,2'-disulfonic acid) binding to the human red cell membrane proteins were studied as a function of concentration, temperature and time. Most

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80328b8db07108a90d26e03075ce0129
https://doi.org/10.1007/bf01868957

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The kinetics of intramolecular cross-linking of the band 3 protein in the red blood cell membrane by 4,4′-diisothiocyano dihydrostilbene-2,2′-disulfonic acid (H2DIDS)

Autor: Sigrid Lepke, Lutz Kampmann, Hugo Fasold, Günter Fritzsch, Hermann Passow

Publikováno v: The Journal of Membrane Biology. 70:199-216

The two isothiocyanate groups of the anion transport inhibitor 4,4'-diisothiocyano dihydrostilbene-2-2'-disulfonate (H2DIDS) may react covalently with two lysine residues called a and b that reside on the chymotryptic 60,000 Dalton and 35,000 Dalton

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41b78ab0a44fd81b503bcdfefcb4ab05
https://doi.org/10.1007/bf01870563

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