| PrP | <protein> PrPc is a normal protein anchored to the outer surface of neurons and, to a lesser extent, the surfaces of other cells, including lymphocytes. The prion thought to be responsible for scrapie and other spongiform encephalopathies is hypothesised to be a modified form of PrPc, PrPSc. (18 Nov 1997) |
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| prp 27-30 protein | Protease-resistant core of prpsc, the abnormal isoform of prion proteins (prions). Prp 27-30 is produced by limited proteolysis of the n-terminus of prpsc. (12 Dec 1998) |
| prpc proteins | Normal cellular isoform of prion proteins (prions) encoded by a chromosomal gene and found in normal and scrapie-infected brain tissue, and other normal tissue. Prpc are protease-sensitive proteins whose function is unknown. Posttranslational modification of prpc into prpsc leads to infectivity. (12 Dec 1998) |
| PRPP | <abbreviation> 5-phospho-alpha-d-ribosyl 1-pyrophosphate. (05 Mar 2000) |
| PRPP synthetase | <enzyme> An enzyme that catalyses the reaction of alpha-d-ribose-5-phosphate and ATP to produce PRPP and AMP; a regulatory enzyme in purine and pyrimidine biosynthesis; enhanced activity of this enzyme results in an increase in purine biosynthesis leading to gout. (05 Mar 2000) |
| prpsc proteins | Abnormal isoform of prion proteins (prions) resulting from a posttranslational modification of the cellular prion protein (prpc proteins). Prpsc are disease-specific proteins seen in certain human and animal neurodegenerative diseases (prion diseases). (12 Dec 1998) |