His American doctor had taken a medical history and attributed his condition to the two years spent working in a drycleaners when he was 16 and exposed to the solvent trichloroethylene. He set out to prove the association. He discovered that this solvent could cause a latent poisoning and began compiling a case against the manufacturers, ICI, who he claimed knew of the dangers as early as the 1930s.
Right up until his death he worked tirelessly with his son Ben on his research; writing to successive Prime Ministers, politicians, the Department for Environment Food and Rural Affairs and scientists. Unfortunately, a combination of having no academic background and controversial views meant that his work was often dismissed. However, he published his much-referenced findings on the Internet from 1996 onwards and in several publications including the Journal ‘Medical Hypotheses’. He was invited to become a fellow of the New York Academy of Sciences in 1988. ....
Anthony Royal Gerry died from cancer on 16th December 2002 leaving wife Rema, and from previous marriages, two daughters and three sons
fedup2 said:I will admit that I know very little about this so don't read to much into this question. The information on that site was over 5 yrs old. Has there been any new research since then to dispute any of this? No hidden agenda here, just wondering.
Neurodegenerative diseases such as Alzheimer's, Parkinson's and the transmissible spongiform encephalopathies (TSEs) are characterized by abnormal protein deposits, often with large amyloid fibrils. However, questions have arisen as to whether such fibrils or smaller subfibrillar oligomers are the prime causes of disease1, 2. Abnormal deposits in TSEs are rich in PrPres, a protease-resistant form of the PrP protein with the ability to convert the normal, protease-sensitive form of the protein (PrPsen) into PrPres (ref. 3). TSEs can be transmitted between organisms by an enigmatic agent (prion) that contains PrPres (refs 4 and 5). To evaluate systematically the relationship between infectivity, converting activity and the size of various PrPres-containing aggregates, PrPres was partially disaggregated, fractionated by size and analysed by light scattering and non-denaturing gel electrophoresis. Our analyses revealed that with respect to PrP content, infectivity and converting activity peaked markedly in 17−27-nm (300−600 kDa) particles, whereas these activities were substantially lower in large fibrils and virtually absent in oligomers of 5 PrP molecules. These results suggest that non-fibrillar particles, with masses equivalent to 14−28 PrP molecules, are the most efficient initiators of TSE disease.
PrP content of PrP-res aggregates
Based on protein assays and ultra-microbalance measurements, 47±9% of the vacuum-dried weight of the washed, unfractionated SUS-treated PrP-res particles was protein (data not shown), and, according to semi-quantitative western blots (data not shown), >87% of the protein was PrP. Adjusting for the glycan and glycophosphatidylinositol content (~25%) of PK-treated PrP molecules, we estimate that at least 54% of the mass was attributable to PrP molecules
reader (the Second) Thanks MLA and Tam. :roll: :roll: [/quote said:I think I just discovered what it means to be collateral damage! :?
Thanks for what, reader2?
Oh well, you're welcome!
If you liked it, I'll try to do more of it.