TY  - JOUR
A1  - Askin, Elif
A1  - Emmerich-Fritsche, Angelika
A1  - Goppel, Anna
A1  - Hemmerling, Mario
A1  - Kapaun, Nina
A1  - Lohmann, Georg
A1  - Müller, Sebastian
A1  - Niederberger, Andreas
A1  - Pabel, Katharina
A1  - Putzer, Max
A1  - Roth-Isigkeit, David
A1  - Seidler, Christoph
A1  - Tiedemann, Paul
A1  - Vasel, J. Justus
A1  - Weiß, Norman
T1  - MenschenRechtsMagazin : Informationen | Meinungen | Analysen
N2  - Aus dem Inhalt: - Themenschwerpunkt: Menschenrechte und Staatsbürgerschaft - Gibt es Menschenrechte ohne Bürgerschaft? - Menschenwürde und Staatsbürgerschaft - Die General Comments des Menschenrechtsausschusses der Vereinten Nationen – ein Beitrag zur Rechtsentwicklung im Völkerrecht - Politische Selbstbestimmung als Menschenrecht und im Völkerrecht - Libyen und der von außen unterstützte Systemwechsel
T3  - MenschenRechtsMagazin : MRM ; Informationen, Meinungen, Analysen - 17.2012/2 
Y1  - 2012
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus-62122
SN  - 1434-2820
VL  - 17
IS  - 2
PB  - Universitätsverlag Potsdam
CY  - Potsdam
ER  - 
TY  - JOUR
A1  - Stalz, Holger
A1  - Roth, Udo
A1  - Schleuder, Detlev
A1  - Macht, Marcus
A1  - Haebel, Sophie
A1  - Strupat, Kerstin
A1  - Peter-Katalinic, Jasna
A1  - Hanisch, Franz-Georg
T1  - The Geodia cydonium galectin exhibits prototype and chimera-type characteristics and a unique sequence polymorphism within its carbohydrate recognition domain
N2  - The ancestral galectin from the sponge Geodia cydonium (GCG) is classified on a structural basis to the prototype subfamily, whereas its carbohydrate-binding specificity is related to that of the mammalian chimera-type galectin-3. This dual coordination reveals GCG as a potential precursor of the later evolved galectin subfamilies, which is reflected in the primary structure of the protein. This study provides evidence that GCG is the LECT1 gene product, while neither a previously described LECT2 gene nor a functional LECT2 gene product was found in the specimen under investigation. The electrophoretically separated protein isomers with apparent molecular masses of 13, 15, and 16 kDa correspond to variants of the LECT1 protein-exhibiting peptide sequence polymorphisms that concern critical positions of the carbohydrate recognition domain (13 kDa: Leu51, Asn55, His130, Gly137; 15 kDa: Ser51, Asn55, Asn130, Gly137; 16 kDa: Ser51, Tyr55, Asn130, Glu137). Four residues, highly conserved in the galectin family, are substituted. None of the residues claimed to be involved in interactions with GalNAc alpha 1-3 moieties at an extended binding subsite of galectin-3 was identified in the corresponding positions of GCG. Apparently, the substitutions do not confer distinct binding characteristics to the GCG variants as evidenced by binding studies with a recombinantly expressed 15-kDa isoform. The natural isoforms as well as the recombinant 15-kDa isoform oligomerize by the formation of non-covalent heteromeric or homomeric complexes. A phosphorylation of the galectin was confirmed neither by mass spectrometry nor by alkaline phosphatase treatment combined with isoelectric focusing
Y1  - 2006
UR  - http://glycob.oxfordjournals.org/content/16/5/402.full
U6  - https://doi.org/10.1093/glycob/cwj086
ER  - 
TY  - JOUR
A1  - Liebeck, Bernd Michael
A1  - Hidalgo, Natalia
A1  - Roth, Georg
A1  - Popescu, Crisan
A1  - Böker, Alexander
T1  - Synthesis and characterization of Methyl Cellulose/Keratin Hydrolysate Composite Membranes
JF  - Polymers / Molecular Diversity Preservation International
N2  - It is known that aqueous keratin hydrolysate solutions can be produced from feathers using superheated water as solvent. This method is optimized in this study by varying the time and temperature of the heat treatment in order to obtain a high solute content in the solution. With the dissolved polypeptides, films are produced using methyl cellulose as supporting material. Thereby, novel composite membranes are produced from bio-waste. It is expected that these materials exhibit both protein and polysaccharide properties. The influence of the embedded keratin hydrolysates on the methyl cellulose structure is investigated using Fourier transform infrared spectroscopy (FTIR) and wide angle X-ray diffraction (WAXD). Adsorption peaks of both components are present in the spectra of the membranes, while the X-ray analysis shows that the polypeptides are incorporated into the semi-crystalline methyl cellulose structure. This behavior significantly influences the mechanical properties of the composite films as is shown by tensile tests. Since further processing steps, e.g., crosslinking, may involve a heat treatment, thermogravimetric analysis (TGA) is applied to obtain information on the thermal stability of the composite materials.
KW  - bio-based
KW  - composite materials
KW  - methyl cellulose
KW  - keratin
KW  - superheated water
Y1  - 2017
U6  - https://doi.org/10.3390/polym9030091
SN  - 2073-4360
VL  - 9
PB  - MDPI
CY  - Basel
ER  - 
TY  - BOOK
A1  - Amend-Traut, Anja
A1  - Bayerle, Katrin
A1  - Duncker, Arne Dirk
A1  - Dusil, Stephan
A1  - Forster, Wolfgang
A1  - Frassek, Ralf
A1  - Hermann, Hans-Georg
A1  - Koch, Elisabeth
A1  - Lettmaier, Saskia
A1  - Löhning, Martin
A1  - Ludyga, Hannes
A1  - Maetschke, Matthias
A1  - Mayenburg, David von
A1  - Meder, Stephan
A1  - Repgen, Tilman
A1  - Roth, Andreas
A1  - Saar, Stefan Christoph
A1  - Schlinker, Steffen
A1  - Schmoeckel, Matthias
A1  - Schumann, Eva
A1  - Thier, Andreas
T1  - Familienrecht §§ 1297-1921
T3  - Historisch-kritischer Kommentar zum BGB ; 4
Y1  - 2018
SN  - 978-3-16-156399-7
PB  - Mohr Siebeck
CY  - Tübingen
ER  -