This looks to be a major advance. The full text will be of great interest.
Use of capillary electrophoresis and fluorescent labeled peptides to detect
the abnormal prion protein in the blood of animals that are infected with a
transmissible spongiform encephalopathy.
Schmerr MJ email@example.com, Jenny AL, Bulgin MS, Miller JM,
Hamir AN, Cutlip RC, Goodwin KR
J Chromatogr A 1999 Aug 20;853(1-2):207-14
National Animal Disease Center, MWA, ARS, US Department of Agriculture,
Ames, IA 50010, USA.
Transmissible spongiform encephalopathies in humans and in animals are
fatal neuro-degenerative diseases with long incubation times. The putative
cause of these diseases is a normal host protein, the prion protein, that
becomes altered. This abnormal prion protein is found mostly in the brains
of infected individuals in later stages of the disease, but also can be
found in lymphoid and other tissues in lower amounts. In order to eradicate
this disease in animals, it is important to develop a system that can
concentrate the abnormal prion protein and an assay that is very sensitive.
The sensitivity that can be achieved with capillary electrophoresis makes
it possible to detect the abnormal protein in blood. A peptide from the
carboxyl terminal region, amino acid positions 218-232, was labeled at the
amino terminus with fluorescein during the synthesis of the peptide.
Antibodies that have been produced to this peptide were affinity purified
and used in a capillary electrophoresis immunoassay. The amount of
fluorescein labeled peptide in the capillary was 50 amol.
Blood was obtained from normal sheep and elk, from sheep infected with
scrapie and elk infected with chronic wasting disease. Buffy coats and
plasma were prepared by a conventional method. After treatment with
proteinase K, which destroys the normal protein but not the altered one,
the blood fractions were extracted and tested in the capillary
electrophoresis immunoassay for the abnormal prion protein.
The abnormal prion protein was detected in fractions from blood from
infected animals but not from normal animals. This assay makes a
pre-clinical assay possible for these diseases and could be adapted to test
for the abnormal prion protein in process materials that are used for
manufacture of pharmaceuticals and products for human consumption.
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