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      Identification of glycoinositol phospholipid-linked and truncated forms of the scrapie prion protein

      , , ,
      Biochemistry
      American Chemical Society (ACS)

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          Abstract

          Analysis of carboxy-terminal peptides derived from endoproteinase Lys-C digests of the scrapie isoform of the hamster prion protein revealed that the majority of the molecules are glycoinositol phospholipid linked through ethanolamine attached at serin-231. However, approximately 15% of PrPSc had a carboxy-terminal peptide that ends at glycine-228. It is intriguing that this glycine is part of the PrP sequence Gly-Arg-Arg, which is an established target sequence for the proteolysis and release of bioactive peptides from larger precursors. The mechanism of formation, as well as the role of the truncated carboxy terminus in the dissemination and neuropathology of scrapie, remains to be determined.

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          Author and article information

          Journal
          Biochemistry
          Biochemistry
          American Chemical Society (ACS)
          0006-2960
          1520-4995
          September 1990
          September 1990
          : 29
          : 38
          : 8879-8884
          Article
          10.1021/bi00490a001
          1980209
          341acc53-8dce-45e1-94a4-0ae414d239e4
          © 1990
          History

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