Application of a time-resolved fluoroimmunoassay for the analysis of normal prion protein in human blood and its components

Ian MacGregor; James Hope; Geoff Barnard; Louise Kirby; Olive Drummond; Duncan Pepper; Valerie Hornsey; Robin Barclay; Hagop Bessos; Marc Turner; Christopher Prowse

doi:10.1159/000031082

Application of a time-resolved fluoroimmunoassay for the analysis of normal prion protein in human blood and its components

Ian MacGregor, James Hope, Geoff Barnard, Louise Kirby, Olive Drummond, Duncan Pepper, Valerie Hornsey, Robin Barclay, Hagop Bessos, Marc Turner, Christopher Prowse

School of Biological Sciences

Research output: Contribution to journal › Article › peer-review

Abstract

Background and Objectives: To quantify the cellular isoform of prion protein (PrP(c)) in human blood using a new time-resolved dissociation-enhanced fluoroimmunoassay (DELFIA®). Materials and Methods: The DELFIA was optimised for human blood samples and applied to isolated cell and plasma fractions from blood donations. The physicochemical properties of PrP(c) were analysed. Results: 26.5% of blood PrP(c) was associated with the platelet fraction, 0.8% with polymorphonuclear leucocytes, 2.4% with mononuclear leucocytes, 1.8% with red cells and 68.5% with plasma (mean values from 4 processed donations). Conclusion: The majority of blood PrP(c) is found in the platelet and plasma compartments.

Original language	English
Pages (from-to)	88-96
Number of pages	9
Journal	Vox Sanguinis
Volume	77
Issue number	2
DOIs	https://doi.org/10.1159/000031082
Publication status	Published - Sept 1999

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10.1159/000031082

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title = "Application of a time-resolved fluoroimmunoassay for the analysis of normal prion protein in human blood and its components",

abstract = "Background and Objectives: To quantify the cellular isoform of prion protein (PrP(c)) in human blood using a new time-resolved dissociation-enhanced fluoroimmunoassay (DELFIA{\textregistered}). Materials and Methods: The DELFIA was optimised for human blood samples and applied to isolated cell and plasma fractions from blood donations. The physicochemical properties of PrP(c) were analysed. Results: 26.5% of blood PrP(c) was associated with the platelet fraction, 0.8% with polymorphonuclear leucocytes, 2.4% with mononuclear leucocytes, 1.8% with red cells and 68.5% with plasma (mean values from 4 processed donations). Conclusion: The majority of blood PrP(c) is found in the platelet and plasma compartments.",

author = "Ian MacGregor and James Hope and Geoff Barnard and Louise Kirby and Olive Drummond and Duncan Pepper and Valerie Hornsey and Robin Barclay and Hagop Bessos and Marc Turner and Christopher Prowse",

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T1 - Application of a time-resolved fluoroimmunoassay for the analysis of normal prion protein in human blood and its components

AU - MacGregor, Ian

AU - Hope, James

AU - Barnard, Geoff

AU - Kirby, Louise

AU - Drummond, Olive

AU - Pepper, Duncan

AU - Hornsey, Valerie

AU - Barclay, Robin

AU - Bessos, Hagop

AU - Turner, Marc

AU - Prowse, Christopher

PY - 1999/9

Y1 - 1999/9

N2 - Background and Objectives: To quantify the cellular isoform of prion protein (PrP(c)) in human blood using a new time-resolved dissociation-enhanced fluoroimmunoassay (DELFIA®). Materials and Methods: The DELFIA was optimised for human blood samples and applied to isolated cell and plasma fractions from blood donations. The physicochemical properties of PrP(c) were analysed. Results: 26.5% of blood PrP(c) was associated with the platelet fraction, 0.8% with polymorphonuclear leucocytes, 2.4% with mononuclear leucocytes, 1.8% with red cells and 68.5% with plasma (mean values from 4 processed donations). Conclusion: The majority of blood PrP(c) is found in the platelet and plasma compartments.

AB - Background and Objectives: To quantify the cellular isoform of prion protein (PrP(c)) in human blood using a new time-resolved dissociation-enhanced fluoroimmunoassay (DELFIA®). Materials and Methods: The DELFIA was optimised for human blood samples and applied to isolated cell and plasma fractions from blood donations. The physicochemical properties of PrP(c) were analysed. Results: 26.5% of blood PrP(c) was associated with the platelet fraction, 0.8% with polymorphonuclear leucocytes, 2.4% with mononuclear leucocytes, 1.8% with red cells and 68.5% with plasma (mean values from 4 processed donations). Conclusion: The majority of blood PrP(c) is found in the platelet and plasma compartments.

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Application of a time-resolved fluoroimmunoassay for the analysis of normal prion protein in human blood and its components

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