NR ACOC
AU Cherepenko,E.I.
TI [Prions: on the enzymatic function of PrPc from mammalian and prion "families"]
OT Priony: ob enzimaticheskoi funktsii PrPc mlekopitaiushchikh i prionnykh "semenakh".
QU Ukrainskii Biokhimicheskii Zhurnal 2002 Mar-Apr; 74(2): 5-9
PT journal article; review; review, tutorial
AB This minireview deals with some approaches and results of experiments which enabled to discover SOD-like activity of the mammal PrP protein. This activity required the unchanged region of the repeated octapeptide and Cu2+ binding to the appropriate sites of the PrP molecule. It was shown that an infectious prion isoform could bind the normal isoform. This leads to the loss of PrP SOD-like function accompanied by Cu2+ release from the molecule. Also, the problem of sowing the protein seeds of prion propagation is briefly summarized and the first evidence of abnormal protein conformation induced in vivo using yeast cell and in vitro formed Sup 35 prion seed is described.
ZR 20
MH Animal; English Abstract; Mammals; Phosphoprotein Phosphatase/metabolism/*physiology; Superoxide Dismutase/*metabolism
AD Institute of Molecular Biology and Genetics of NAS of Ukraine, Kyiv. maliuta@imbig.kiev.ua
SP russisch
PO Ukraine