Abstract:
:Cellular prion protein, PrP(C), is essential for the development of prion diseases where it is considered to be a substrate for the formation of the disease-associated conformer, PrP(Sc). In sheep, PrP(C) is abundant in neuronal tissue and is also found at lower concentrations in a range of non-neuronal tissues, including mammary gland. Here, we demonstrate the presence of soluble PrP(C) in the non-cellular, non-lipid fraction of clarified ovine milk. Compared with brain-derived PrP(C), ovine milk PrP(C) displays an increased electrophoretic mobility. Ovine milk PrP(C) is mainly present as three species that differ in the extent of their N-linked glycosylation, with glycoform profiles varying among animals. Similar PrP(C) species are also present in fresh and commercial homogenised/pasteurised bovine milk, with additional N-terminal PrP(C) fragments detectable in ruminant milk and commercial milk products.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Maddison BC,Whitelam GC,Gough KCdoi
10.1016/j.bbrc.2006.12.006subject
Has Abstractpub_date
2007-02-02 00:00:00pages
195-9issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(06)02649-0journal_volume
353pub_type
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