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| Home > Publications database > New hope for the diagnosis and therapy of Alzheimer's disease |
| Journal Article | PreJuSER-56233 |
2007
Bentham Science Publ.
Schiphol
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Please use a persistent id in citations: doi:10.2174/092986607780363970
Abstract: Improperly folded metal cofactor-containing proteins (e.g., copper chaperone for Superoxide dismutase, CCS) are believed to play a key role in several protein-misfolding diseases (e.g., Alzheimer's disease or Amyotrophic Lateral Sclerosis) because Under regular physiological conditions, metallochaperolles activate or stabilize the native conformation of important metalloproteins (e.g., superoxide dismutase) in certain Cellular processes. For an improved diagnosis and therapy of neurodegenerative diseases, new methodologies have to be developed that enable a well-defined differentiation between properly folded and inactive metalloproteins in clinical samples. In the literature it is reported that different high molecular mass metal-containing proteins were isolated in brain samples from Alzheimer's patients and in vegetables by using a 2-dimensional polyacrylamide gel electrophoresis (2-DE) procedure. In the present article, selected results of these studies are Scrutinized and compared with some results obtained by a standardized method termed 'quantitative preparative native continuous polycrylamide gel electrophoresis (QPNC-PAGE)'. Conclusively, QPNC-PAGE is a highly efficient approach used by biochemists to resolve native and denatured metalloproteins (MW 6 - >= 200 kDa) in complex protein Mixtures.
Keyword(s): J ; QPNC-PAGE (auto) ; 2-DE (auto) ; GPC (auto) ; NMR (auto) ; CCS (auto) ; Alzheimer's disease (auto) ; isoelectric point (auto) ; native conformation (auto) ; breakthrough method (auto) ; biofluids (auto) ; cadmium protein (auto) ; folding (auto) ; Arabidopsis (auto) ; metal cofactor (auto) ; get structure (auto)
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