id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-253783-3a1qde41	Johnson, Christopher J	Prions Adhere to Soil Minerals and Remain Infectious	2006-04-14		.txt	text/plain	5461	283	51	We examined the potential for soil to serve as a TSE reservoir by studying the interaction of the disease-associated prion protein (PrP(Sc)) with common soil minerals. X-ray diffraction analysis provided no evidence that PrP Sc entered Mte interlayer spaces (Mte d 001 spacings were 1.22 nm and 1.47 nm before and after PrP Sc adsorption, respectively); prion protein appeared to adsorb to only external clay surfaces. Prion protein desorbed from Kte and quartz did not exhibit a change in molecular mass ( Figure 1A ), suggesting that surface properties specific to Mte were responsible for the cleavage. To control for any unbound prion protein that may have cosedimented with Mte particles, mineral-free PrP Sc suspensions were processed in the same manner as in sorption experiments. Our results demonstrate that all soil mineral surfaces examined bound PrP Sc and that Mte and quartz have larger specific binding capacities for PrP Sc than does Kte (Figure 1 ).	./cache/cord-253783-3a1qde41.txt	./txt/cord-253783-3a1qde41.txt