[Diagnosis of bovine spongiform encephalopathy and scrapie by western blot]

The rabbits were immuned with bovine prion protein (BoPrPC) which was expressed in E. coli and anti-PrPC antibody (T1) was obtained. According to pathological prion protein (PrPSC) was resistant to protease treatment, extracts of brain tissue were digested with proteinase K and detected by western blot with T1 antibody. The results showed that protease-resistant pathological PrPSC was existed in golden hamster brain tissue which was inoculated with scrapie strain 263 K, but no protein existed in normal golden hamster brain homogenates which was detected with T1 antibody. Several bovines and sheep from Beijing were used for diagnosis of Bovine spongiform encephalopathy (BSE) and scrapie, their brain tissue were freshly collected and homogenated. The homogenates were separated on SDS-PAGE and detected by western blot with T1 antibody. The results indicated no protease-resistant protein(PrPSC) existed, this suggested they were not infected by BSE and scrapie. The same results were obtained with 1A8 antibody from England. These results indicated we could detect BSE and scrapie with T1 antibody.