Abstract
We developed a competitive enzyme-linked immunosorbent assay (ELISA) to detect prion protein contained in materials derived from cattle, aiming at establishing a method to detect abnormal prion protein (PrPSc) in food products. Rabbit polyclonal antibodies were raised against bovine prion peptides. Using these antibodies, we have established a competitive ELISA that is capable of detecting recombinant bovine prion protein (rBoPrP) in the range of 12 to 1,200 ng and we used it to determine prion protein contents in bovine cerebral cortex. This assay system was evaluated by spiking food products with various amounts of rBoPrP. The determination gave 2-fold higher values in minced meat homogenates and lower values in large intestine homogenates than the values expected from the spiked amounts. This assay provides a simple determination method of spiked rBoPrP, and therefore is expected to be useful for investigating sample pretreatment methods.
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