Abstract
The histones including H2a, H2b, H3 and H4 purified from pig liver tissue were immobilized onto Sepharose 4B to create a histone-Sepharose column. During chromatography of cow milk casein by histone-Sepharose column, two isoforms of prion protein (PrP(c)) with 34 and 30kDa molecular mass corresponding to diglycosylated and monoglycosylated PrP(c) respectively were found to be captured by histone ligands. To further verify the interaction between histones and PrP(c), the PrP(c)-Sepharose column was prepared and used to separate the histones. Two chromatography processes and SDS-PAGE demonstrated that only H3 in the histones was found to interact with PrP(c). This study suggested H3 could be the target molecule of PrP(C) in nuclei, which might be useful for understanding the prion disease.
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