کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1938075 | 1050731 | 2007 | 5 صفحه PDF | دانلود رایگان |

Cellular prion protein, PrPC, is essential for the development of prion diseases where it is considered to be a substrate for the formation of the disease-associated conformer, PrPSc. In sheep, PrPC 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 PrPC in the non-cellular, non-lipid fraction of clarified ovine milk. Compared with brain-derived PrPC, ovine milk PrPC displays an increased electrophoretic mobility. Ovine milk PrPC is mainly present as three species that differ in the extent of their N-linked glycosylation, with glycoform profiles varying among animals. Similar PrPC species are also present in fresh and commercial homogenised/pasteurised bovine milk, with additional N-terminal PrPC fragments detectable in ruminant milk and commercial milk products.
Journal: Biochemical and Biophysical Research Communications - Volume 353, Issue 1, 2 February 2007, Pages 195–199