Dr. Günther Enderlein (–) whose main book Bacteria Cyclogeny was published in Enderlein was a visionary thinker who made. Günther Enderlein () saw the healthy host as filled with primitive life Enderlein’s work was the book by the French researcher A. Béchamp, titled. Dr Gunther Enderlein’s research has revealed the following: The cell is not the smallest visible living unit, but rather the colloid. This colloid has been termed the .

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In addition, human beings have: Science also has identified the building blocks of carbohydrates as sugars, such as glucose and fructose, needed for energy synthesis, Importantly, ATP adenosine triphosphate is the general currency of energy enferlein all living organisms.

In the human body, ATP is hydrolyzed to ADP adenosine diphosphatewhich provides energy for walking, thinking, hearing, seeing and other functions.

Günther Enderlein

If a person did not recycle ATP, then the body would need to produce 74 kg of this substance per day. Humans also need carbohydrates for energy storage in glycogen, which is stored in the liver and muscles [54]. The building blocks of lipids are fatty acids, glycerol and several other molecules.

Lipids are required for biomembranes. Every living organism is composed of cells, which is surrounded by a membrane comprised of lipids and proteins [55] [56]. Moreover, nucleic acids are needed for DNA, the storage of genetic information, and for transferring genetic information to RNA, from which the information is taken to make a protein. The building blocks for nucleic acids are nucleotides [57]. Finally, tunther molecular weight substances are required, which include trace elements, minerals and vitamins [58].

The Synthesis of Proteins Enderlein proposed a protein of plant origin protit that can multiply by itself.

But how are proteins created? Biosynthesis of proteins occurs in all living organisms. The amino acids are put together step by step to form a poly-peptide chain consisting of many of the 20 amino acids required in the human body.

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Finally, the protein grows to a three-dimensional structure and develops its function [59]. The Prion Perspective What about Prions, which are classified as protein diseases? Science knows that if infected cattle brain is fed to sheep, the animals will develop Scrapie, which is related to Mad Cow Disease.

It also is known that the protein in the normal physiological stage forms an alpha-helix. In Prion disease, the protein changes configuration to the so-called beta-sheet, enabling them to stick together and precipitate in the brain, which causes the cells to die, creating large holes in the brain. Do all the hazardous proteins all come from the infected cattle brain eaten by the sheep? The answer is no.

The infected protein that was eaten may induce a change in configuration from alpha helix to beta sheet, transforming the endogenous protein into a toxic one. The ingested prions are sufficient to trigger this pathogenic process [61]. Importantly, the protein does not multiply by itself. Modern knowledge of cell structure and composition shows that this progression is impossible.

[Günther Enderlein 95 years old].

For example, a T bacteriophage is a protein coat with a single strand of DNA. A virus by itself cannot multiply. It infects a cell, incorporating its own little amount of DNA into the host chromosome, and recruits the host protein machinery to make new viruses [62].

The much higher developed organisms of bacteria, such as Bacillus subtilis, possess a plasma membrane, cell wall and circular chromosome within the cell plasma, but no organelles. All metabolic processes occur in the cell plasma [63]. Finally, fungi such as the yeast S. Each compartment is separated from the others by membranes. Consequently, the number of genes coding for specific proteins also vary greatly. The genome of viruses comprise 5 to genes [65], the bacteria Bacillus subtilis has 4, genes [66] and the yeast S.


As a result, a spontanous transition from virus to bacteria to a fungus is simply not possible. This progression took billions of years of evolution, with the concomitant formation of a huge number of other species. Nevertheless, based on the research of his day, it is understandable how Enderlein came enderleni his conclusions. Endetlein changes so rapidly that a hypothesis made today can be verified or falsified within months or few years.

Science uses a background of knowledge to interpret events. However, any conclusion depends on precise experiments being conducted. It is enderlei important to get correct results to gain new knowledge. Of course, after more than 75 years, scientific knowledge is very different from what was known during Enderlein’s days.

Today, DNA and proteins can rapidly be identified. The determined DNA sequence or the identified protein delivers conclusive information on the origin and nature of the structures viewed in enderrlein blood.

Experimental Approach What is the modern scientific hypothesis on Enderlein’s so-called protits or Darkfield Bodies? If protits are unknown living organisms, they should: If protits are not living organisms, they could be: Only if a protein has the proper structure can it develop its proper biological function.

If the proper structure is disturbed, it is known that proteins coagulate and then precipitate; 5 a specific polymerization of one or more host proteins, not foreign proteins. To distinguish between these five possibilities, Proteom research was conducted by Christopher Gerner, Ph. Proteom research represents the most modern, scientific approach presently available to examine proteins, and enables the observer to identify different metabolic conditions by looking at the concentration of proteins.

According to the five hypotheses, the following three Proteom research results can be expected: If new protein spots appear after cultivation that cannot be detected in the freshly made preparation, this strongly argues for the growth of an unknown organism that metabolizes the host’s own protein to amino acids.

This organism in turn uses these amino acids to produce its own protein.

This can be best explained gunyher degradation of proteins by proteases present in the preparation. This would argue for Darkfield Bodies being unspecific protein aggregation. This would argue for a specific polymerization of body-own proteins.

As a result, it is possible to distinguish whether enderein not growth or reproduction is taking place. Methods The protein samples were loaded onto a matrix capable of separating different proteins according to their size and charge via Two-dimensional Gel Electrophoresis. After staining, the matrix was scanned into a computer, which automatically compared it to scientific databases that provided information on which proteins spots were known, which were new, and which gained or lost intensity.

In Two-dimensional Gel Electrophoresis, ebderlein protein in the first dimension is separated by charge. Dependent on its charge, a protein moves to a specific position. The second dimension separates the proteins by size. For example, if different proteins are in the same position in the first dimension, they can be separated according to their size in the second dimension.

Results To distinguish between the five postulated hypotheses, Darkfield Bodies were yunther from human blood according to the method developed by Dr. These Darkfield Bodies, which Enderlein called macrosymprotits or symprotits, morphologically compare to the ones observed in native blood.

One sample tunther taken from the freshly made preparation, a second sample after one day, and a third after three days of culture. After one day, many tiny protein spots resembling Darkfield Bodies could be seen when viewed by phase contrast microscopy Figure 1 b.


After three days of cultivation, the spots that were morphologically idetified as so-called symprotits gained in mass Figure 1 c [69]. It appeared clearly that something guntther growing or increasing in size from tiny spots up to larger spots. To distinguish between a living organism and protein aggregation, all the samples were examined by high-resolution Two-dimensional Gel Electrophoresis to compare the protein pattern of cultured samples taken after one and three days.

Figure 2 shows the comparison of the two-dimensional protein patterns of the starting material to the cultured Darkfield Bodies. Picture a shows the starting material, whereas pictures b and c show cultured Darkfield Bodies before and after purification. The cultured Darkfield Bodies Figure 2, picture b show a similar protein pattern to the starting material Figure 2, picture a.

The serum protein albumin is very dominant. It is known that albumin is highly soluble with a great affinity to proteins. To eliminate albumin from unsoluble Darkfield Bodies, purification steps were performed. The cultivated Darkfield Bodies were purified with detergents Sodiumdodecylsulfate, Tween 40as well as high and low salt gumther. Under these conditions, plasma membranes would dissolve readily. Phase contrast microscopy revealed that the purification had no influence on the morphology of the Darkfield Bodies.

This indicates that the Darkfield Bodies are not living organisms because of the lack of a plasma membrane. Figure 2, picture c reveals that albumin could be separated from the cultivated Darkfield preparation.

This indicates that albumin most probably binds to the surface of Darkfield Bodies. In addition, the protein spot of globin significantly increased in size larger spot in comparison to the unpurified Darkfield Bodies, showing that Darkfield Bodies are specific polymerization products primarily composed of the body’s own molecules globin and albumin [69].

If protits and symprotits are a specific aggregation of globin, then it should be possible to stain these structures with an antibody that specifically recognizes globin. To investigate this possibility, immunofluorescent staining experiments were performed.

Darkfield Bodies specifically stained positive with globin antibodies [70]. This provided final proof that globin is the primary constituent part of Darkfield Bodies. Discussion Now that Proteom research has proven that symprotits and macrosymprotits are actually clusters of globin, it is important to explain the source of this globin. To maintain proper homeostasis, old and damaged erythrocytes are selectively removed from the bloodstream by spleen and liver cells, which recognize a change in shape comformation of a membrane receptor band 3 protein on the red cells.

This yunther is caused by oxidative damage to hemoglobin. The red blood cells are forced through capillaries, causing mechanical stress because the diameter of capillaries is smaller than the diameter of a red blood cell.

A constant rearrangement of the plasma membrane and protein skeleton takes place within the cell. If the cell is oxidatively damaged, it cannot rearrange the plasma membrane rapidly enough to meet these conditions This mechanical stress causes cell lysis to occur.

Consequently, hemoglobin is set free in the sera Figure 3, a. As hemoglobin is released, the serum protein haptoglobin specifically gunthdr to hemoglobin and transports it to the liver, where it is degraded. The haptoglobin is then recycled to the sera in a rapid process so that it can collect more hemoglobin physiologic protection mechanism Figure 3, c.

As erythrocytes undergo cell lysis, iron is easily oxidized by serum components.