Kratzin, Hartmut Dieter

[["dc.bibliographiccitation.firstpage","16711"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","16719"],["dc.bibliographiccitation.volume","276"],["dc.contributor.author","Kramer, Michael L."],["dc.contributor.author","Kratzin, H. D."],["dc.contributor.author","Schmidt, B."],["dc.contributor.author","Romer, A."],["dc.contributor.author","Windl, Otto"],["dc.contributor.author","Liemann, S."],["dc.contributor.author","Hornemann, S."],["dc.contributor.author","Kretzschmar, Hans A."],["dc.date.accessioned","2018-11-07T09:03:42Z"],["dc.date.available","2018-11-07T09:03:42Z"],["dc.date.issued","2001"],["dc.description.abstract","The prion protein is known to be a copper-binding protein, but affinity and stoichiometry data for the full-length protein at a physiological pH of 7 were lacking. Furthermore, it was unknown whether only the highly flexible N-terminal segment with its octarepeat region is involved in copper binding or whether the structured C-terminal domain is also involved, Therefore we systematically investigated the stoichiometry and affinity of copper binding to full-length prion protein PrP23-231 and to different N- and C-terminal fragments using electrospray ionization mass spectrometry and fluorescence spectroscopy. Our data indicate that the unstructured N-terminal segment is the cooperative copper-binding domain of the prion protein. The prion protein binds up to five copper(II) ions with half-maximal binding at similar to2 muM. This argues strongly for a direct role of the prion protein in copper metabolism, since it is almost saturated at about 5 muM, and the exchangeable copper Fool concentration in blood is about 8 muM."],["dc.identifier.doi","10.1074/jbc.M006554200"],["dc.identifier.isi","000168730400018"],["dc.identifier.pmid","11278306"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24953"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.title","Prion protein binds copper within the physiological concentration range"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4357"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Proteomics"],["dc.bibliographiccitation.lastpage","4366"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Brechlin, Peter"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Steinacker, Petra"],["dc.contributor.author","Cepek, Lukas"],["dc.contributor.author","Kratzin, Hartmut"],["dc.contributor.author","Lehnert, Stefan"],["dc.contributor.author","Jesse, Sarah"],["dc.contributor.author","Mollenhauer, Brit"],["dc.contributor.author","Kretzschmar, Hans A."],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Otto, Markus"],["dc.date.accessioned","2018-11-07T11:10:48Z"],["dc.date.available","2018-11-07T11:10:48Z"],["dc.date.issued","2008"],["dc.description.abstract","So far only the detection of 14-3-3 proteins in cerebrospinal fluid (CSF) is included in the diagnostic criteria for sporadic Creutzfeldt-jakob disease (sCJD). However, this assay cannot be used for screening because of the high rate of false positive results in sCJD, and often negative results in variant CJD. To facilitate the differential diagnosis of CJD, we applied 2-D differential gel-electrophoresis (2-D DIGE) as a quantitative proteomic screening system for CSF proteins. We compared 36 patients suffering from sCJD with 30 patients suffering from other neurodegenerative diseases. Sample preparation was optimized in consideration of the fact that CSF is composed of blood- and brain-derived proteins, and an improved 2-D DIGE protocol was established. Using this method in combination with protein identification by MALDI-TOF-MS, several known surrogate markers of sCJD like 14-3-3 protein, neuron-specific enolase, and lactate dehydrogenase were readily identified. Moreover, a not yet identified protein with an approximate molecular mass of 85 kDa was found as marker for sCJD with high diagnostic specificity and sensitivity. We conclude that our proteomic approach is useful to differentiate CJD from other neurodegenerative diseases and expect that CSF-optimized 2-D DIGE will find broad application in the search for other brain derived proteins in CSF."],["dc.identifier.doi","10.1002/pmic.200800375"],["dc.identifier.isi","000260717300021"],["dc.identifier.pmid","18814332"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/53290"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-Blackwell"],["dc.relation.issn","1615-9861"],["dc.relation.issn","1615-9853"],["dc.title","Cerebrospinal fluid-optimized two-dimensional difference gel electrophoresis (2-D DIGE) facilitates the differential diagnosis of Creutzfeldt-Jakob disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]