The prion or whatever it is that causes Mad Cow Disease is one tough SOB. On a Nova a couple years ago, Dr Paul Brown said, “These agents are almost immortal. They resist alcohol, they resist boiling, they resist hospital detergents… We exposed it to temperatures that turned it to ash, and it did not entirely kill the agent.”
Why would that be? Is it because the immolaton was not complete? The normal assumption when something is reduced to ash is that there is nothing left with the original structure. Looking at their structure they look real stable. Is that enough to survive cremation?
I’d suggest it’s just a matter of the temperature used. At a sufficiently ‘low’ temperature for combustion, could fragments of the prion sufficient to cause infection survive? Possibly. But one thing is certain, this is simply a protein, and although it may have some powerful secondary structure (meaning folding of the amino acid chain), it will have the same bond energies (on average) in its peptide backbone as all proteins, and as such, will burn at a sufficient temperature ie the thermodynamics of the combustion are the same as for other proteins (strictly I suppose ‘delta’ G is the same, but if anyone wants to take that up, do it by email).
You’d think so, wouldn’t you? I would think that between 1800 and 14,000 degrees F, cremation temperatures according to the Neptune Society, any protein will be reduced to its constituent atoms. But on 20-20 (I think) a couple weeks ago they showed airplane hangers full of contaminated bone meal and the announcer said that they couldn’t burn them because the ashes would still be infective. How can any protein be that tough?
