THE USE OF CAPILLARY ELECTROPHORESIS TO DETECT AND CHARACTERIZE THE PRION PROTEIN EXTRACTED FROM SCRAPIE INFECTED SHEEP. (CONF.TSE: MANAGING RISK IN MAMMALIAN ORGANS..SPON. BY NMHCC,WASHINGTON,DC)

Authors: Schmerr, Mary Jo; JENNY, ALLEN - NVSL,AMES,IA; Cutlip, Randall

Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: 2/25/1997
Publication Date: N/A
Citation: N/A

Interpretive Summary:

Technical Abstract: Scrapie in sheep and in goats is the prototype of transmissible spongiform encephalopathies (TSE) that are characterized by neurodegeneration and eventually death. A feature of these diseases is the accumulation in the brain of rod shaped fibrils that form from an aggregated protein. We are developing new methods for extraction of the protein that is involved in the formation of these fibrils. The efficiency of extraction by biologica buffers is rather low. We are investigating the use of organic solvent extraction in conjunction with high performance liquid chromatography to improve yields. We will use these methods to extract tissues from sheep including lymph nodes tonsils, brain, and spleen. Because of its versatility, capillary electrophoresis will be used to characterize the proteins present in the extracts and to test for the presence of prion protein. A competition immunoassay using fluorescent labeled peptides from the prion protein with laser induced fluorescence for detection will be used to detect the presence of prion protein. Capillary isoelectric focusing and SDS-gel capillary electrophoresis will be used to further characterize the samples.