1/17/23 Teleconference - What is Bravo, what is imuno, how do they work together?

This call is intended to share experience with the products.

This is the recording of the call. Please feel free to ask questions at mimi@healthyenergetics.com



Bravo Bootcamp - http://simplymimi.net/archives/1400

imuno Bootcamp

Semi Related Articles -


Edestiny -

Edestin protein:
* aids digestion
* is relatively phosphorus free
* is considered the backbone of the cell’s DNA
* is similar to the human body’s own globular proteins found in blood plasma
* produces antibodies which are vital to maintain a healthy immune system.
* resembles the globulin in blood plasma
* Is compatible with the human digestive system

Perhaps it is a common denominator for getting signals transferred through the following systems:
* digestion
* DNA transmissions
* Blood communications
* Antibodies in the immune system


A new study shows . . .
imuno® is over 100 times more effective than pure GcMAF
If your clinic or doctor doesn’t use imuno in their clinic give them this information and have them please contact us for our exclusive products.
19th February 2020: Dr Marco Ruggiero, MD. PhD.
Elevated serum alpha-N-acetylgalactosaminidase (nagalase) is associated with a number of life threatening and/or debilitating conditions ranging from cancer (Korbelik et al., 1998; Greco et al., 2009; Thyer et al., 2013) to viral infections caused by influenza virus and HIV (Yamamoto and Urade, 2005; Yamamoto, 2006), bacterial infections (Caines et al., 2008), alcoholism (Zoga et al., 2017), and autism (Bradstreet et al., 2012).
Nagalase, an enzyme, was first proposed as a marker for cancer and viral infections and its increased serum activity in these conditions was associated with immune system deficiency because nagalase prevents formation of the Gc protein derived Macrophage Activating Factor (GcMAF), an immune stimulant cytokine (Yamamoto and Naraparaju, 1997; Yamamoto and Urade, 2005; Yamamoto, 2006). According to the original hypothesis proposed by Yamamoto and Colleagues, cancer cells and cells infected by viruses produced and released nagalase that caused immune deficiency that, in turn, favored the progression of cancer or viral infections. Therefore, elevated serum nagalase activity in cancer and viral infections was considered a consequence of cancer or viral-infected cells releasing nagalase.
In apparent agreement with this hypothesis, successful immunotherapy of cancer with GcMAF was associated with a decrease of serum nagalase activity (Thyer et al., 2013; Schwalb et al., 2016) that was attributed to the effects of GcMAF on macrophages that, once activated, attacked cancer cells with consequent decrease of the number of cancer cells producing nagalase.
This interpretation, however, was contradicted by the observation that in autism, just like in cancer, successful immunotherapy with GcMAF was associated with significant decrease of serum nagalase activity (Bradstreet et al., 2012). Since the autistic subjects successfully treated with GcMAF had no signs of cancer cells producing nagalase, nor of any other concurrent disease or infections (Bradstreet et al., 2012), a novel hypothesis concerning the role of nagalase was proposed. According to this novel hypothesis, elevated nagalase activity has to be considered more a pathogenetic factor for cancer and other conditions rather than a simple marker.
In simpler words, elevated nagalase activity may be one of the causative factors leading to cancer, autism or other diseases because elevated nagalase impairs the function of the immune system and immune deficiency plays a pivotal role in the onset and development of cancer and other diseases. Such a role for nagalase is now well established as exemplified by the title of a recent review that reads " Is α-N-acetylgalactosaminidase the key to curing cancer?" (Saburi et al., 2017a). Based on these considerations, strategies aiming at reducing serum nagalase activity may prove useful in the fight against cancer, autism, viral infections and all other conditions associated with elevated serum nagalase activity
How GcMAF works:
Here we demonstrated for the first time that GcMAF directly binds to, and inhibits, human nagalase in vitro, thus elucidating the mechanism of action of GcMAF and explaining its effectiveness in a variety of conditions ranging from cancer to autism (Saburi et al., 2017a; Saburi et al., 2017b; Bradstreet et al., 2012; Greilberger and Herwig, 2020). In addition, we demonstrate that a novel supplement containing low-molecular-weight microbial chondroitin sulfate, ultrapure phosphatidylcholine, and vitamin D3, (imuno®, imuno Corporation, Vanuatu) shows more than 100 fold higher activity than purified GcMAF.
How the GcMAF was tested:
Human nagalase and GcMAF were purified at R.E.D. Laboratories (Zellik, Belgium). The
experiment was performed using microtiter plates coated with a specific antibody able to capture human nagalase. Samples were incubated with a standardized dilution of a pool of 300 human sera from healthy subjects and, after 1 h incubation and exhaustive washing, nagalase-GcMAF or nagalase-imuno® complexes were detected with a horse radish peroxidase conjugate of a rabbit antibody. In order to establish the kinetics of interaction between nagalase and GcMAF, or imuno®, the serum pool was mixed either with 200 ng of purified Gc-MAF, or with a 1:100 dilution of imuno® in phosphate buffered saline (PBS). Since preliminary experiments indicated that undiluted imuno® exceeded the binding capacity of nagalase in the test, imuno® was diluted 1:100 in PBS. The mixture was then incubated at room temperature for 4, 24, 48, 72 and 120 h. Values for nagalase binding activity in the absence of GcMAF or imuno®, with only PBS in the reaction mixture, were taken as  1.00. The experiment was repeated twice and the results reported in Fig. 1 are the means of the two experiments.

As shown in Fig. 1, purified GcMAF bound human nagalase only after 4 h incubation, reached a peak at 48 h, and returned below baseline values at 120 h. imuno®, on the other hand, had an initial value (at 0 h) higher than PBS, thus demonstrating immediate, intrinsic GcMAF activity against human nagalase. At every time point, imuno® showed significantly higher activity in comparison with purified GcMAF and, at 120 h, imuno® activity was still well above baseline, thus indicating a stronger, more prolonged activity. It is worth noticing that imuno® was diluted 100 fold and, therefore, it may be argued that its activity against human nagalase is more than 100 fold higher than that of purified GcMAF.
It is also important to consider that these results were obtained in vitro, that is in the absence of any variable or confounding factor that may hamper interpretation of results observed in clinical settings. Direct interaction between imuno® and nagalase may help explaining the effectiveness of imuno® recently observed by Antonucci and Colleagues in those conditions where GcMAF had proven effective in the past (Antonucci et al., 2019a; Antonucci et al., 2019b) and lead to propose imuno® as a more potent and intrinsically safer substitute for human-blood-derived GcMAF. The significantly higher potency of imuno® is to be ascribed to its peculiar molecular design that was described in detail in two recent papers (Ruggiero and Pacini, 2018a; Ruggiero and Pacini, 2018b); in brief, imuno® reproduces that physical-chemical features of GcMAF at a much higher molecular efficiency and density. The N- acetylgalactosamine active site of GcMAF is present in much higher concentration in imuno® thanks to the presence of low-molecular-weight chondroitin sulfate, a sulfated polysaccharide that is composed by an alternating chain of Nacetylgalactosamine and glucuronic acid. The hydrophobic moieties of GcMAF, that are the regions binding vitamin D and fatty acids, are present in imuno® thanks to the binding of phosphatidylcholine to chondroitin sulfate. Vitamin D3, essential for increasing the potency of GcMAF as demonstrated by Greilberger and Herwig in 2020, is intercalated in the proto-cellular structure formed by the core of chondroitin sulfate surrounded by phosphatidylcholine (Ruggiero and Pacini, 2018a). In fact, imuno® was designed taking into account the physical-chemical features of GcMAF that were published 2013 when a molecular model of GcMAF interaction with the cell membrane was described (Thyer et al., 2013). In this model, optimal interaction was achieved when GcMAF was non-covalently bound to a fatty acid - in that example, oleic acid - and vitamin D3 that are the conditions reproduced, at a much higher molecular efficiency and density, in imuno®.

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Bravo Yogurt is Recognized
by Anti-Aging Authority
You may know, Dr. David A. Sinclair, PhD, Professor at Harvard Medical School.  He is the world's authority in the field of anti-aging medicine.  He authored seminal articles in major scientific journals as well as a New York Times Best Selling book.  
Well, it turns out that he is one of us!!  He enjoys his Bravo Yogurt every morning!
Without any solicitation from us, as Dr Ruggiero  has never met him, Dr Sinclair told the world that he uses Bravo Yogurt every morning as part of his anti-aging/wellness protocol.  The excerpt of his interview is here.
Dr. Ruggiero is the inventor of Bravo Yogurt and is deeply interested in studying anti-aging.  He believes that we as people should have more capacity to endure.  He has studied lobsters who don’t die of old age and cancer which can stay alive in a petri dish for 60 years.  He thinks that we can change our fates and has put his ideas to work in a product of longevity.  
I am quite sure that this book by Dr. David A. Sinclair, PhD, Professor at Harvard Medical School is a book worth reading and practices worth noting.  For example, use your Bravo yogurt every morning.  Make it a daily part of your very long life!   www.bravocoop.com

Explore Bravo & imuno’s unique properties
to protect you from viral epidemic
Dr Marco Ruggiero has recently communicated that imuno and Bravo are ideally suited to help with the coronavirus.
Bravo, thanks to its unique composition in phages (friendly viruses that fight pathogenic viruses) and its proven efficacy on empowering the immune system may be used to help prevent infection by the coronavirus that is causing the current epidemic.
As you know, the phages in Bravo are known to fight a number of pathogenic viruses that include HIV, and it was recently demonstrated that the coronavirus responsible for the current epidemic, contains HIV sequences that are responsible for its infectivity and are the target of Bravo's phages https://www.biorxiv.org/content/10.1101/714154v2.
Dr. Ruggiero says, "I take the liberty to write that I am 99% (100% would be unrealistic) confident that imuno will help with the coronavirus for two reasons.  The first and most obvious is its general effect on the immune system as described in all the papers where it has been mentioned."
"The second is related to the specific anti-viral properties of chondroitin sulfate that are further amplified by the molecular arrangement of imuno.  As you may know by now, the coronavirus responsible for the current epidemic attacks human cells because it has spikes from HIV that no one knows, at the present, whether they were intentionally inserted or are result of a casual viral recombination. (highly improbable but not impossible)"
Needless to say, the chondroitin sulfate in imuno is much more potent/bioavailable that the molecules used in those studies for at least two reasons: it is homogeneous and low-molecular-weight; it is arranged in a supramolecular structure that makes it more bioavailable and efficient in binding to the HIV spikes.
Because of these evidences, I am 99% sure that imuno will work against coronavirus.
Combination with Bravo may prove synergistic as we have observed in the case of myeloma and in the case of Dr. Carter that I have just submitted to the Am J Immunol.
Bravo will work through the phages and the natural GcMAF and it will complement the effects of imuno. Most likely, Bravo and imuno will work even if administered alone, but the combination may prove synergistic.


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