NR AIXC
AU Nishino,S.; Kishita,A.; Nishida,Y.
TI Alternative origin for "gain-of-function" by mutant SOD enzyme and for conformational change of normal prion protein
QU Zeitschrift für Naturforschung. Section C. Journal of Biosciences 2001 Nov-Dec; 56(11-12): 1144-9
PT journal article
AB Capillary electrophoresis and ESI-Mass spectrometry methods have revealed that a hydroperoxo-copper(II) complex with (tpa) (=tris(2-pyridylmethyl)amine) reacts with carbonic anhydrase or amyloid beta-peptide (1-40) as a nucleophile to induce the conformational change of the protein structure, while the Cu(bdpg)-complex ((bdpg)=N,N-bis(2-pyridylmethy)-beta-alanineamide) acts as an electrophile toward the proteins to degrade them under the same experimental conditions. This will lead to suggest that enhanced nucleophilic attack by a copper(II)-peroxide adduct to peptide bonding may be one of the serious origins for the "gain-of-function" by mutant superoxide dismutase and for conformational change of normal prion protein.
MH Electrophoresis, Capillary; Prions/*chemistry; Protein Conformation; Spectrometry, Mass, Electrospray Ionization; Superoxide Dismutase/chemistry/*genetics
AD Chemical Institute for Neurodegeneration (CIN), Department of Chemistry, Faculty of Science, Yamagata University, Japan.
SP englisch
PO Deutschland