Purification of normal cellular prion protein from human platelets and the formation of a high molecular weight prion protein complex following platelet activation.

Abstract:

:A method for the extraction and purification of PrP(C), in its native monomeric form, from outdated human platelet concentrates is described. Both calcium ionophore platelet activation and lysis in Triton X-100 were evaluated as methods for the extraction of soluble platelet PrP(C) in its monomeric form. Following platelet activation, the majority of released PrP(C) was detected as a disulphide linked high molecular weight complex, which under reducing conditions could be separated into what appear to be stable non-disulphide linked PrP dimers or PrP covalently linked to another as yet unidentified protein. This phenomenon appears to be unique to activation since only monomeric PrP(C) was detected following lysis of resting platelets. Subsequently, PrP(C) was purified from the Triton X-100 lysate by sequential cation ion exchange and Cu2+ affinity chromatography. From 10 L of outdated platelet concentrate, we were able to recover 1.29 mg PrP(C) at a purity of 92%.

authors

Jones M,Head MW,Connolly JG,Farquhar CF,Hornsey VS,Pepper DS,MacGregor IR

doi

10.1016/j.bbrc.2005.07.045

subject

Has Abstract

pub_date

2005-09-16 00:00:00

pages

48-56

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)01523-8

journal_volume

335

pub_type

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