Avery long time ago I assembled and posted some information that I had gleaned from approximately 200 pages of scientific data meant for education purposes. I condensed the material that I thought was appropo to Parkinson's disease. It ended up being about 1 1/2 pages long, and it was filled with "SCIENCE WORDS!!!!" Well, in my excitement, I forgot to identify the source, and as hard as I tried, I could not locate it on the internet. Guess what. Due to googles wonderful search engine I located it. It all came together that night at 3 a.m. This was not written to specifically address Parkinson's disease, but I believe that if it were used as a guide for discovery the key to recovery would be found. Here it is again. (Thank you Paula)

I FOUND IT, I FOUND IT, I FOUND IT!!!!!!!! ONE REASON WHY THE NEURONS DIE!!!!!!!!!!!! SOME OF THE POSSIBLE CULPRITS AND HOW THEY DO IT!!!!!!!!!!!!!!!!!!!! A METHOD OF IDENTIFYING OTHERS!!!!!!!!!! TAKE A LOOK----IT IS DOCUMENTED, SCIENTIFIC DATA AND NOT SPE CULATION ON MY PART!!!!!!!!! START POLISHING YOUR DANCING SHOES!!!!!!!

Quote:

: "58.What is a cytochrome? (Notes, 36) The cytochromes are electron acceptors which as a class are heme-containing proteins which mediate Fe+++/Fe++ one-electron transfers. There are five cytochromes with increasing electron accepting potentials. The heme in cytochromes b, c1, and c are Fe-protoporphyrin IX which is also the prosthetic group in myoglobin and hemoglobin. It is covalently attached to the protein in these cytochromes. 59.Which cytochrome is responsible for the reduction of molecular oxygen? (Notes, 36) Cytochrome oxidase. Contains cytochromes a and a3 as a complex, they are the terminal electron transport carriers. Each have a different prosthetic group, heme A, but th e same basic Fe-tetrapyrrole structure. It also contains two copper atoms which alternate between Cu++ and Cu+. Electron transfer through cytochrome oxidase is inhibited by cyanide or CO which appear to bind very tightly to the cytochrome a3 moiety. 60.Wha t type of structure is protoporphyrin IX? Where does it occur? (Notes, 36) The heme in cytochromes b, c1, and c are Fe-protoporphyrin IX which is also the prosthetic group in myoglobin and hemoglobin. It is covalently attached to the protein in these cytoc hromes. 61.What are several agents which inhibit electron transfer in the process of oxidative phosphorylation? (Notes, 33) It is of scientific and medical interest to note a number of chemicals which inhibit electron transport at different sites. The leth ality of cyanide and carbon monoxide depends upon the selective blockage of cytochrome oxidase. Cyanide binds to the ferric form of iron of the (a) cytochromes and carbon monoxide binds to the ferrous form. The antibiotic antimycin A blocks electron flow a t site two (cytochrome reductase), wheras rotenone and amytal block electron transfer within the NADH-Q reductase complex (below). Blockage at any site interrupts the generation of a proton gradient (below), and ATP synthesis is inhibited. Blockage sites: 62.Define the "uncoupling" of oxidative phosphorylation. What are several agents which uncouple oxidative phosphorylation? (Notes, 38) The chemiosmotic theory is supported by observations that compounds capable of disrupting a proton gradient across the in ner mitochondrial membrane effectively UNCOUPLE oxidative phosphorylation. "Uncoupling" means that electron flow and oxygen reduction proceeds without simultaneous formation of ATP. 2,4-dinitrophenol (DNP) and other phenolic compounds are effective uncouplers. These lipophilic compounds transfer protons across the inner mitochondrial membrane, breaking down the proton gradient. 63.How does cyanide inhibit oxidative phosphorylation? How does carbon monoxide inhibit oxidative phosphorylation? (Notes, 33) The lethality of cyanide and carbon monoxide depends upon the selective blockageof cytochrome oxidase. Cyanide binds to the ferric form of iron of the (a) cytochromes and carbon monoxide binds to the ferrous form. 64.Brifly describe the "Chemosmotic Hypotheses " of oxidative phosphorylation. (Notes, 37) The coupling of OXIDATION and PHOSPHORYLATION is indirect. Briefly stated: 1.protons are pumped from the inner to the outer side of the inner mitochondrial membrane during electron transport. 2.the inner membrane is not freely permeable to protons so an electromotive potential is established across this membrane. 3.a transmembrane multisubunit enzyme ATP synthetase (intrinsic to themitochondrial membrane) converts ADP to ATP as outermembrane protons re-enter themi tochondria through a channel coupled to ATP synthase. Supported by evidence of the pH gradient which exists across the inner mitochondrial membrane.... "

I didn't say it was easy to understand. Are you excited, michael?? You betcha!!! michael oops. I forgot to give the source: So, what has caused me to come to this conclusion? First, what is that conclusion? I have concluded that a class of substances that can potentially cause Parkinson's disease, has been identified and profiled. By using that profile, we should be able to identify other substances with the same profile and test them to see if they do indeed cause Parkinson's or Parkinson's like symptoms. It's like reducing a haystack down to a handfull of hay. What brought me to this conclusion? Well, toni ght I started thinking about some of the products that I have used (alternatives) that have given me significant improvement. I realized that most of them had Hydrogen in their formulas. I then looked at what goes on in the mitochondria, and I realized tha t Hydrogen is a key element in the production of ATP, the energy of the cell. I then saw that NADH gave up its Hydrogen in the process, so in my mind, it is a hydrogen donor. That is what I called it, anyway. I did a Google search on Hydrogen donors, and there they were, along with Hydrogen Acceptors. "Hmmmmmmmm" I said. Then, I asked myself, "What are some Hydrogen Acceptors?" Guess what I found in the list. I found, among others, Iron, Manganese, copper, and Rotenone. Every one of these are suspected as possible causes of PD., but I have never seen anything that said they were in any way related. Next, I wondered if there were a way to identify other such substances. Low and behold, there is a database into which one can submit a specific profile Query , and it will spit out the names of substances that match that profile. By this time I was really getting excited. Next, I learned that many of these substances can be neutralized. WOWZERS!!! Do you know what that means?? That's how I see it, anyway. I think that we can reverse this disease in many if not most cases.

And finally, here is the website:

http://www.cartercenter.org/resource...ephti/library/
lecture_notes/health_science_students/MedicalBiochemistry.pdf

By the way, all of this fits perfectly with the lysosomal malfunction explanation that Paula wrote above and wha olsen posted in another thread.