Presented by THE ROBERT CATHEY RESEARCH SOURCE http://www.europa.com/~rsc ------------------------------------------------------------------------- Enzyme Therapy and Cancer Resolution As mentioned before, as far as the cancer cell is concerned, what's wanted is a formulation that would accentuate Amylase or the glycogen/starch digesting enzyme over the proteolytic enzymes like trypsin, chymotrypsin or bromelin and papain, which currently predominate in all so-called "immuno-enzyme" or "metabolic" protocols in treating cancer. This is wrong, and here's why: Graphic depiction: (-)(-)(-)(-)(-)(-)(-)(-)(-)(sialic acid side-chains) (o)(o)(o)(o)(o)(o)(o)(o)(o)(o)(o)(o) (Carbohydrates) +++++++++++++++++++++++++++(Protein molecules) xxxxxxxxxxxxxxxxxxxxxxxxxxx(inside of cell) This represents the cross-section of a cancer cell membrane. The outer or "presenting" surface is represented by negative signs (sialic acid) underlayered by positive charges (proteins, the "backbone"), and within this merely a convenient symbol for cell contents. Proteolytic enzymes cannot get at the membrane associated proteins, lipoproteins, etc. until the sialic acid rich carbohydrates have been degraded by the starch-glycogen-saccharide digesting enzymes. The enzymes in question being lead principally by pancreatic amylase. Only then can the protein degrading enzymes in the arsenal have any relevance as far as the "backbone" of the cancer cell are concerned. The proteolytic enzymes carboxypeptidase, trypsin, chymotrypsin, etc. will begin their work after the "blanket" or "jelly" coat has been stripped away. All the enzymes are important and each do different things at different times. Obviously timing and proportion are important for best results. Order of structure in the substrate determines what acts first in the enzyme complement. No one that I know of applies the enzyme protocol in the order just delineated. The plasma membrane is a glyco-protein, and presents sugary side chains outwardly, and these mask the proteins, and lipo-proteins and phospholipids. Also, people have expressed concern about taking "too many enzymes" for fear they'll digest their normal tissues. The phospho-lipid barriers of normal cells will not be harmed by these enzymes. Exactly why is not fully understood. Beard believed it was because they are of the wrong shape to act as substrates for endogenous enzymes; while inert connective tissues are protected by inhibitors normal to the soma. There is no way that even 500,000 units of pancreatic trypsin or amylase will somehow "digest" normal living tissues. Dead tissues, yes. The commonest side effect from using these is a result of the release of immune-complexes. These are the anti-body-antigen units that have never been "eaten" up by macrophage or degraded by endogenous enzymes. Thus inflammatory reactions may arise or even symptoms similar to fibro-myalgia may arise; but generalized inflammation and fibro-myalgia itself are successfully treated by enzyme therapy. All of these same enzymes will degrade the diffusing glyco-proteins or hormones secreted by the cancer cell, but the steroids are acted on additionally by the lysosomal enzyme beta-glucuronidase. Remember, John Beard and Dr. Lambelle found that amylase used in a proportion of AT LEAST 2 TO 1 (amylase 2; protease 1) worked best; while they would not even consider any "trypsin" treatment of cancer at all. They never used purely "proteolytic" approaches. But modern experimentors think they've found a better way apparently. Beard recommended as much amylase as could be applied, so that if one used 1000 units of trypsin, then 2,000 or 12,000 units amylase would be best. The accessibility of enzymes in Beard's day made this hard to acheive. I hope this post makes a little clearer why this enzyme is most important. We are able to advise people wishing to purchase optimal enzymes. Contact the author at: rsc@navi.net --------------------------------------------------------------------------- Disclaimer. This Web page was written and made by Roger Cathey, Research Associate of the ROBERT CATHEY RESEARCH SOURCE. All pages Copyright © 1996 R.S.Cathey, except where specified otherwise.