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• W1996356104 abstract "Prion diseases are characterized by the intraneuronal accumulation of a pathological isoform (PrPSc) of host-encoded prion protein (PrPC). While PrPScdisplays a partial resistance, PrPCis easily degraded by this enzyme. As it turned out in our experiments, PrPCof six species is initially degraded to an intermediate fragment of 25-28 kDa prior to complete proteolysis which was solely detected by antibodies binding to epitopes carboxy-terminally of amino acid 144 of PrPC. The intermediate fragment thus lacked the amino-terminus of PrPC. These findinds are well in line with the putative structure of PrPC: the amino-terminus consists of a highly flexible and thus more proteinase K sensitive tail while the carboxy-terminus is folded into possibly more resistant α-helices and β-sheets. We observed significant differences in the PK sensitivities of PrPCfrom six different species and from three ovine PrP alleles, while no remarkable variation was seen in PrPCfrom six regions of an ovine brain. This indicates that variations in the sequence of PrP may alter its three-dimensional structure and consequently change its sensitivity towards proteolytic enzymes." @default.
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• W1996356104 date "1998-12-01" @default.
• W1996356104 modified "2023-09-23" @default.
• W1996356104 title "Cellular Prion Proteins of Mammalian Species Display an Intrinsic Partial Proteinase K Resistance" @default.
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• W1996356104 doi "https://doi.org/10.1006/bbrc.1998.9838" @default.
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