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Oxygen Therapy

PostPosted: Sat Jul 01, 2017 10:26 am
by sacrosanct
Hi folks,

I just wanted to mention something I tried and couldn't get to work. Maybe if we all did this, we could bounce off each other's ideas and find a viable solution. I'd like to see some science in the solutions people come up with, rather than hocus pocus old wives tails about certain herbs or supplements that might be useful.

I try lots of things, so I'll update you all if I find something worth a mention.

Here's the science =>

First of all it is based from a simple fact which we know to be true. We know microbial TMA production only occurs anaerobically. I wanted to know why this is . . . .

So I read the DMB paper found here =>

http://www.sciencedirect.com/science/ar ... 7415016293

The paper indicates that two enzymes are required to actually cleave Choline into Trimethylamine and Acetaldehyde. They are termed Choline UTlisation (Cut) CutC and CutD. The paper runs permutations of the bacteria with only one of enzymes at a time (CutC/CutD) spliced into them and determines that both enzymes have to be present in order for Choline TMA lyase activity to occur.

I wanted to see what these enzymes were, so read the reference paper for the actual structure and functional characterisation of CutC. This paper and research was only published/performed in 2015. That paper can be found here =>

https://www.ncbi.nlm.nih.gov/pubmed/26187464

The paper identifies CutC as a Glycly Radical Enzyme (GRE) and CutD as an activating enzyme. There is actually a common family of GRE's that have been thoroughly characterised over the past 25 years or so. Based on that research, the paper concludes that =>

"Along with the activating enzyme CutD, CutC cleaves choline, forming TMA and acetaldehyde under anaerobic conditions. Under aerobic conditions, catalysis is impossible because the glycyl radical readily reacts with oxygen, cleaves the main chain, and irreversibly inactivates the enzyme"

This is the reason Choline TMA lyase only occurs anaerobically. In the presence of oxygen, the CutC glycyl radical, like the other GRE's, is actually fragmented in two, rendering it useless.

For this research the paper cites another paper, proving the other GRE's (in this case Pyruvate Formate lyase) fragment in the presence of diatomic oxygen =>

https://www.ncbi.nlm.nih.gov/pmc/articl ... 7-0212.pdf

It is possible to buy slow releasing oxygen supplements. They usually come in the form of Magnesium Peroxide, which slowly releases oxygen in the digestive tract in the presence of stomach acid. They are sold as 'Colon Cleanses' as the oxygen is actually designed to kill anaerobic bacteria in the intestines. Whether they actually perform this bactericidal function is irrelevant. Providing they do actually release oxygen, it should theoretically destroy the CutC enzyme produced by TMA forming bacteria, inhibiting Choline TMA lyase from actually occurring. No Choline TMA lyase, no trimethylamine.

The issues I had with this are as follows =>

I found no evidence that the products I tried (OxyPowder) actually release oxygen. Moreover Magnesium is a strong laxative, meaning consuming large quantities will see you in the bathroom, a lot :-)

I also tried H2O2 (Hydrogen Peroxide) in small quantities. The issues with this are that Oxygen in any form other than the diatomic form found in the the atmosphere has an odour. O3 (Ozone) and H2O2 both have pungent bleach like aromas. Hence even if the oxygen did destroy the CutC glycly radical, you would still smell of bleach :-)

Has anyone else had success with any kind of oxygen therapy?