Important contributions of a new quantitative preparative native continuous polyacrylamide gel electrophoresis (QPNC-PAGE) procedure for elucidating metal cofactor metabolisms in protein-misfolding diseases--a theory.
The quantitative analysis of metallochaperone proteins in biofluids (e.g. blood, liquor) may be a major prerequisite for clinical investigations concerning the structure-function relationships of biologically-active metal cofactor-containing chaperones in protein-misfolding diseases (e.g. Alzheimer's or related diseases). For these purposes, a new state-of-the-art gel electrophoresis [quantitative preparative native continuous polyacrylamide gel electrophoresis procedure (QPNC-PAGE)] combined with biological mass and NMR spectrometries might essentially contribute to provide fundamental insights into the metabolisms of important metal cofactors in biological systems and the proper folding of metallochaperones in conformational diseases.
Kastenholz
Bernd
B
Institute for Chemistry and Dynamics of the Geosphere, Institute III: Phytosphere, Research Centre Juelich, Juelich 52425, Germany. b.kastenholz@fz-juelich.de
D000544:Alzheimer Disease / Q000378:metabolism / Q000473:pathology; D003067:Coenzymes / Q000737:chemistry / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods*; D006801:Humans; D008667:Metalloproteins / Q000737:chemistry / Q000378:metabolism; D008670:Metals / Q000737:chemistry*; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding
D003067:Coenzymes; D008667:Metalloproteins; D008670:Metals; D018832:Molecular Chaperones