@article{MuellerScheer1970,
  author    = {M{\"u}ller, R. and Scheer, Ulrich},
  title     = {Klangspektrographische Untersuchungen der Laut{\"a}ußerung beim Krallenfrosch, Xenopus laevis},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40529},
  year      = {1970},
  abstract  = {No abstract available},
  language  = {de}
}
@article{UlrichsSchangKelleretal.1984,
  author    = {Ulrichs, Karin and Schang, T. and Keller, R. and M{\"u}ller-Ruchholtz, W.},
  title     = {Reactivity of pancreas islet cells with antisera of known specificity},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-45466},
  year      = {1984},
  abstract  = {No abstract available},
  language  = {en}
}
@article{UlrichsKellerMuellerRuchholtz1985,
  author    = {Ulrichs, Karin and Keller, R. and M{\"u}ller-Ruchholtz, W.},
  title     = {Serological demonstration and manipulation of passenger cells (PC) in pancreas islet grafts},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-72944},
  year      = {1985},
  abstract  = {No abstract available},
  subject      = {Immunobiologie},
  language  = {en}
}
@article{LausUlrichsMuellerRuchholtz1986,
  author    = {Laus, R. and Ulrichs, Karin and M{\"u}ller-Ruchholtz, W.},
  title     = {Molecular Specificity of Human Heterophile Antibodies (HHA) in Normal Human Serum (NHS) Reacting with Xenogeneic Cells.},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-72921},
  year      = {1986},
  abstract  = {No abstract available},
  subject      = {Immunobiologie},
  language  = {en}
}
@article{KochDegerKlotzetal.1986,
  author    = {Koch, R. and Deger, A. and Klotz, Karl-Norbert and Schenzle, D. and Kr{\"a}mer, H. and Kelm, S. and M{\"u}ller, G. and Rapp, R. and Weber, U.},
  title     = {Characterization of solubilized insulin receptors from rat liver microsomes. Existence of two receptor species with different binding properties},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60215},
  year      = {1986},
  abstract  = {Insulin receptors were solubilized from rat liver microsomes by the nonionic detergent Triton X-100. After gel filtration of the extract on Sepharose CL-6B, two insulin-binding species (peak I and peak li) were obtained. The structure and binding properties of both peaks were characterized. Gel filtration yielded Stokes radii of 9.2 nm (peak I) and 8.0 nm (peak Il). Both peaks were glycoproteins. At 4°C peak 1 showed optimal insulin binding at pH 8.0 and high ionic strength. In contrast, peak li bad its binding optimum at pH 7.0 and low ionic strength, where peak I bindingwas minimal. For peak I the change in insulin binding under different conditions of pH and ionic strength was due to a change in receptor affinity only. For peak 11 an additional change in receptor number was found. Both peaks yielded non-linear Scatchard plots under most of the buffer conditions examined. At their binding optima at 4 oc the high affinity dissociation constants were 0.50 nM (peak I) and 0.55 nM (peak II). Sodium dodecyl sulfatejpolyacrylamide gel electrophoresis of peak I revealed five receptor bands with Mr 400000, 365000, 320000, 290000, and 245000 under non-reducing conditions. For peak II two major receptor bands with M\(_r\) 210000 and 115000 were found. The peak II receptor bands were also obtained aftermild reduction of peak I. After complete reduction both peaks showed one major receptor band with M\(_r\) 130000. The reductive generation of the peak II receptor together with molecular mass estimations suggest that the peak I receptor is the disulfide-linked dimer of the peak II receptor. Thus, Triton extracts from rat liver microsomes contain two receptor species, which are related, but differ considerably in their size and insulin-binding properties.},
  subject      = {Toxikologie},
  language  = {en}
}
@article{UlrichsKellerMuellerRuchholtz1986,
  author    = {Ulrichs, Karin and Keller, R. and M{\"u}ller-Ruchholtz, W.},
  title     = {Vorkommen und Manipulation von MHC Klasse II Antigenen auf Zellen isolierter Langerhans-Inseln},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-45499},
  year      = {1986},
  abstract  = {No abstract available},
  subject      = {Langerhans-Inseln},
  language  = {de}
}
@article{UlrichsNoethlingKelleretal.1987,
  author    = {Ulrichs, Karin and N{\"o}thling, R. and Keller, R. and Heusermann, U. and M{\"u}ller-Buchholtz, W.},
  title     = {Genetically determined variation of constitutive major histocompatibility complex class II antigen expression in various rat strains and cell types},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-44769},
  year      = {1987},
  abstract  = {No abstract available},
  subject      = {Chirurgie},
  language  = {en}
}
@article{KorthMuellerSustmannetal.1987,
  author    = {Korth, H.-G. and M{\"u}ller, W. and Sustmann, R. and Christl, Manfred},
  title     = {Rearrangement of Free Radicals, XII. ESR Spectroscopic Study of the Ring Opening of the Homobenzvalenyl Radical},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-58376},
  year      = {1987},
  abstract  = {Abstraction of an allylic hydrogen atom in homobenzvalene (4) either in solurion by photolyticaßy generated tert-butoxyl radicals or in an adamantane matrix by X-rays produces the homobcnzvalenyl radical (5). which tbennally rearranps · to tbe tropylium ndical (1). In solution tbe activation cnergy for the rate determined step of the reaction sequence was detennined· to be 13.4 ± O.S kcal/mol.},
  subject      = {Organische Chemie},
  language  = {en}
}
@article{LausUlrichsMuellerRuchholtz1988,
  author    = {Laus, R. and Ulrichs, Karin and M{\"u}ller-Ruchholtz, W.},
  title     = {Carbohydrate-specific human heterophile antibodies in normal human sera that react with xenogeneic cells},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-78271},
  year      = {1988},
  abstract  = {Human heterophile antibodies (HHA) that are present in normal human sera (NHS)play an important role in hyperacute xenograft rejection. The aim of this study was to analyze the occurrence, mode of action and molecular specificity of HHA in NHS that are directed against xenogeneic Iymphocytes (isolated from mouse, rat, guinea pig, rabbit, cattle and pig) and isolated rat pancreatic islets. All sera contained variable amounts of HHA that killed the target cells via the classical complement pathway. The cytotoxic activity of these HHA was specifically inhibited by certain carbohydrates (a-D-melibiose, ß-Iactose, ß-gentiobiose, ß-cellobiose, D-mannose, N-acetyl-ß-D-mannosamine and a-D-rhamnose) and by rat IgM. By means of affinity chromatography with immobilized inhibitors we obtained an antibody preparation of mainly IgG type from NHS (up to 3.5 mg/IO ml serum) that reacted strongly with rat lymphocytes and isolated rat pancreatic islets. Though thus far residual xenospecific antibody activity has remained in the sera even after multiple affinity chromatography, these data suggest that specific elimination of HHA is feasible and that it may be thus possible to overcome a major obstacle to xenotransplantation.},
  subject      = {Immunobiologie},
  language  = {de}
}
@article{EngemannUlrichsThiedeetal.1990,
  author    = {Engemann, R. and Ulrichs, Karin and Thiede, A. and M{\"u}ller-Ruchholtz, W. and Hamelmann, H.},
  title     = {Value of a physiological liver transplant model in rats. Induction of specific graft tolerance in a fully allogeneic strain combination},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-45622},
  year      = {1990},
  abstract  = {No abstract available},
  language  = {en}
}