Removal of prion infectivity

Details Removal of prion infectivity Removal of prion infectivity

2007-08-07

2007-08-07

Carrillo, Sharidan (Department: 1746)

Cleaning and liquid contact with solids

Processes

Miscellaneous

C422S037000, C422S028000, C134S002000, C134S022100, C134S022110, C134S022130, C134S022160, C134S022170, C134S026000, C134S029000, C134S034000, C134S036000

Reexamination Certificate

active

10518471

ABSTRACT:
Prion infectivity adsorbed onto substrates (for example, chromatographic columns used to fractionate blood plasma) is removed by treatment with 2M sodium chloride. Optionally, the substrate is further washed with 0.1 M sodium hydroxide.

REFERENCES:
patent: 5808011 (1998-09-01), Gawryl et al.
patent: 6221614 (2001-04-01), Prusiner et al.
patent: 6720355 (2004-04-01), Prusiner et al.
patent: 6831161 (2004-12-01), Uhlen et al.
patent: 2002/0041859 (2002-04-01), Prusiner et al.
patent: 2003/0086820 (2003-05-01), McDonnell et al.
patent: 2003/0148385 (2003-08-01), Antloga et al.
patent: 2003/0162225 (2003-08-01), James et al.
patent: 2003/0175362 (2003-09-01), Kross et al.
patent: 2003/0198571 (2003-10-01), Lynch
patent: 2004/0171071 (2004-09-01), Stefas
patent: 2005/0050040 (2005-03-01), Theobald et al.
patent: 2006/0096619 (2006-05-01), Foster et al.
patent: 2001-582013 (2003-08-01), None
patent: 2000-043782 (2000-07-01), None
patent: 2001-054736 (2001-08-01), None
Turk , E. et al. “Purification and properties of the cellular and scrapie hamster prion proteins”Bur. J. Biochem. 176: 21-30 (1988).
James, T.L. et al. “Solution structure of the 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform”PNAS94,:10086-10097 (1997).
Safar, J et al. “Eight prion strains have PrPScmolecules with different conformations”Nature Medicine4(10): 1157-1165 (1998).
Polymenidou, M. “A short purification process for quantitative isolation of PrPScfrom naturally occurring and experimental transmissible spongiform encephalopathies”BMC Infectious Diseases2(23) (2002).
Silveria, J.R. et al. “The most infectious prion protein particles”Nature437: 257-261 (2005) (including supplementary information pp. 1-14).
Meyer, R.K. “A monomer-dimer equilibrium of a cellular prion protein (PrPC) not observed with recombinant PrP★”J. Biol. Chem. 275(48): 28081-38087 (2000).
Castilla, J. et al. “In vitro generation of infectious scrapie protein”Cell121: 195-206 (2005).
EEC Regulatory Document, Notes for Guidance: Guidelines for Minimizing the Risk of Transmitting Agents Causing Spongiform Encephalopathy via Medicinal Products,Biologicals20: 155-158 (1992).
Riesner, D. “Biochemistry and Structure of PrPCand PrPSc”British Medical Bulletin66: 21-33 (2003).
Bennion, B. “Protein conformation and diagnostic tests: the prion protein”Clinical Chemistry48(12): 2105-2114 (2002).
Brimacombe et al. “Characterization and polyanion-binding properties of purified recombinant prion protein”,Biochemical Journal342:605-613 (1999).
Dormont, D. “Agents that cause transmissible subacute spongiform encephalopathies”,Biomedicine & Pharmacotherapy(1999).
Pan et al. “Purification and properties of the cellular prion protein from Syrian hamster brain”,Protein Science1:1343-1352 (1992).
Notification of Transmittal of the International Search Report or the Declaration, corresponding to PCT/GB03/02378, mailed Sep. 18, 2003.

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