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09-03-2009, 08:11 AM
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#1
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Understanding of Amino Acids and some ?'s
There are a ton of experts on this board and I am hopeful that some of you may help me to understand something.
If I understand this properly, when we consume protein, the digestion process separates out the amino acids and distributes them to the bloodstream.
I know that in times of need, with the absence of glucose, the body will look for amino acids to convert to glucose (Gluconeogenesis) for energy, and I believe that they can be taken from the bloodstream OR from muscle tissue to accomplish this.
So, if we are either on some form of keto, or a moderate carb diet and we exceed our glucose levels, our bodies in need of glucose, will look for aminos.
I assume that its first choice would be the bloodstream rather than the muscle.
OK, so first, if anything I stated above is incorrect, please correct me.
Now for the question, obviously protein/amino acids are not free calories, if they are not used, they will get stored as fat, correct?
SO, my question is, how exactly does that work?
Do the aminos stay in the plasma for a certain amount of time, and then after that amount of time if they are not used (either converted to glucose or synthesizing muscle) then they are stored as fat?
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09-03-2009, 10:06 AM
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#2
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This may help
http://www.insulinpumpers.org/howto/pfandbs-2.html
Basically calories from protein will end up being used for energy (rather than going towards building muscle if you are in a caloric deficit). Carbs and fats are protein sparing because when you have enough of a combination of the two to provide for your energy need, protein can then be used towards muscle preservation/building.
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09-03-2009, 10:52 AM
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#3
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Quote:
Originally Posted by determined4000
This may help
http://www.insulinpumpers.org/howto/pfandbs-2.html
Basically calories from protein will end up being used for energy (rather than going towards building muscle if you are in a caloric deficit). Carbs and fats are protein sparing because when you have enough of a combination of the two to provide for your energy need, protein can then be used towards muscle preservation/building.
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If thats the case, how does supplementing with BCAA's fit into the equation?
Will they also end up being used up for energy, or are they limited to muscle repair/growth capabilities?
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09-03-2009, 12:35 PM
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#4
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Quote:
Originally Posted by BBTake2
Do the aminos stay in the plasma for a certain amount of time, and then after that amount of time if they are not used (either converted to glucose or synthesizing muscle) then they are stored as fat?
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Great question.
I would need to research it a bit more to give you a very exact answer, but here is a general answer to it...
Your body is in a constant state of flux. As such, AAs are entering the muscle, and exiting it as well.
What happens is that the NET balance of AAs coming in or out of the muscle (i.e. catabolism vs. anabolism) is determined by hormones.
Anabolic hormones, such as insulin and Testosterone, stimulate growth and prevent muscle protein from leaving the muscle....
Catabolic proteins, such as glucagon, allow the protein to leave the muscle.
Chronic elevation of cortisol is also catabolic.
There are many other hormones that are involved in this shift, but that's in general the idea... Some promote one thing, some the other.
When glucose is no longer available, the AAs in the blood are used as energy source and a massive mobilization of energy reserves and muscle protein begins, with a net movement of AAs out of the muscle and into the blood. Then these blood AAs are used for energy until glucose becomes available, at which point the balance is again shifted, and protein muscle is stopped from being moved out of the muscle tissue (again, this is NET not absolute movement).
The whole thing is much more complex, and I am leaving a few things here and there out of the explanation.
To get a better understanding of this, I suggest you read more about catabolism and anabolism, whole-body metabolism, and AA metabolism....
HTH
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-Not a Dr. in Nutrition or any other Human Biology Field-
Fish Scientist / Computer Geek / Gymaholic
---------------------------------------------------------
Ovolactate Pescaterian and scientist.
Last edited by reefpicker; 09-03-2009 at 12:38 PM.
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09-03-2009, 01:48 PM
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#5
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Quote:
Originally Posted by reefpicker
Great question.
I would need to research it a bit more to give you a very exact answer, but here is a general answer to it...
Your body is in a constant state of flux. As such, AAs are entering the muscle, and exiting it as well.
What happens is that the NET balance of AAs coming in or out of the muscle (i.e. catabolism vs. anabolism) is determined by hormones.
Anabolic hormones, such as insulin and Testosterone, stimulate growth and prevent muscle protein from leaving the muscle....
Catabolic proteins, such as glucagon, allow the protein to leave the muscle.
Chronic elevation of cortisol is also catabolic.
There are many other hormones that are involved in this shift, but that's in general the idea... Some promote one thing, some the other.
When glucose is no longer available, the AAs in the blood are used as energy source and a massive mobilization of energy reserves and muscle protein begins, with a net movement of AAs out of the muscle and into the blood. Then these blood AAs are used for energy until glucose becomes available, at which point the balance is again shifted, and protein muscle is stopped from being moved out of the muscle tissue (again, this is NET not absolute movement).
The whole thing is much more complex, and I am leaving a few things here and there out of the explanation.
To get a better understanding of this, I suggest you read more about catabolism and anabolism, whole-body metabolism, and AA metabolism....
HTH
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Very interesting. So I assume when someone mentions nitrogen retention, they are referring to the capacity of the muscles to hang onto the aminos, perhaps by preventing the uncoupling of the aminos through the nitrogen?
I am also assuming this is the reason determined4000, as well as conventional wisdom, states that you cannot build muscle in a calorie deficit.
However, it would make sense to me that if one were on a keto diet, where the body would no longer rely on glucose, assuming the types of activities a person on a keto diet, were doing, say only LISS type activity and low heart rate lifting, I would imagine that the aminos would be more inclined to stay in the muscles?
In keto, protein muscle synthesis should theoretically be independent of calorie deficit, no?
I completely get why you cannot synthesize muscle when in a calorie deficit and relying on glucose, that makes complete sense. Just not quite getting it on the keto side of things.
I am sure the other complexities that I simply don't understand yet come into play in all of this, but I am really trying to grasp all this.
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09-03-2009, 06:04 PM
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#6
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Quote:
Originally Posted by BBTake2
Very interesting. So I assume when someone mentions nitrogen retention, they are referring to the capacity of the muscles to hang onto the aminos, perhaps by preventing the uncoupling of the aminos through the nitrogen?
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If the AA's "uncouple" from the nitrogen, then they stop being AA's. Not sure what "nitrogen retention" means, sounds like a bro term...
Quote:
Originally Posted by BBTake2
I am also assuming this is the reason determined4000, as well as conventional wisdom, states that you cannot build muscle in a calorie deficit.
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Actually, you can go one step further and say that growth in general does not occur on a caloric deficit. Anabolism (construction of new tissue) is unlikely to occur under such conditions because the environment inside the body is mostly catabolic. Hence, malnourishment often leads to underdevelopment and (during critical phases) short stature, etc, delayed puberty etc.
Quote:
Originally Posted by BBTake2
However, it would make sense to me that if one were on a keto diet, where the body would no longer rely on glucose, assuming the types of activities a person on a keto diet, were doing, say only LISS type activity and low heart rate lifting, I would imagine that the aminos would be more inclined to stay in the muscles?
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You are correct, but to get into more details research Muscle-Sparing Protein Diets.
Glucose is still produce, but carbohydrates are not the main source of it. Google the term Gluconeogenesis.
Quote:
Originally Posted by BBTake2
In keto, protein muscle synthesis should theoretically be independent of calorie deficit, no?
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Hmmm.... No.... I don't think so. As I said, it can be understood that to build muscle you need an energy surplus. The question that most people have is if you can take that energy from your fat reserves. IME It seems that newbies are able to do this and I have often wondered about this myself. I think age, hormones, genes, etc might play a role in it... But I would yield to others in here that can provide more info on this.
Again, going from experience, a high protein diet even in surplus will yield the best results. You will be able to build muscle, not gain fat, etc.
Your questions are interesting. I also suggest you look for hypertrophy, as this is the essence of gaining muscle mass. Specifically, there was some talk a while back about a signaling molecule called mTOR that might be linked to "sensing" energy levels, etc. But I can't recall the details. I can give you a good link if you want to know more about it. PM me.
__________________
Dr. ReefPicker (PhD)
-Not a Dr. in Nutrition or any other Human Biology Field-
Fish Scientist / Computer Geek / Gymaholic
---------------------------------------------------------
Ovolactate Pescaterian and scientist.
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09-03-2009, 08:15 PM
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#7
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Quote:
Originally Posted by BBTake2
However, it would make sense to me that if one were on a keto diet, where the body would no longer rely on glucose, assuming the types of activities a person on a keto diet, were doing, say only LISS type activity and low heart rate lifting, I would imagine that the aminos would be more inclined to stay in the muscles?
In keto, protein muscle synthesis should theoretically be independent of calorie deficit, no?
I completely get why you cannot synthesize muscle when in a calorie deficit and relying on glucose, that makes complete sense. Just not quite getting it on the keto side of things.
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Concerning Keto
This explains the theory why fat should be the largest macro in low carb diets (Keto is generally almost/about twice as high in fat as protein)
http://www.second-opinions.co.uk/fat-not-protein.html
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09-03-2009, 09:44 PM
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#8
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learn'n 2 EAT!LIFT!SLEEP!
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Not sure if this will help, but amino acids cannot be stored and only a tiny bit is excreted per day. Basically it can only get 'stored' by synthesising muscle, or basically getting the amino group taken off, shipped off to the liver to be turned into urea and then sent to kidneys to be excreted in our urine. The remaining carbon skeleton can do various things such as get metabolised directly, be used in gluconeogenesis which changes it into glucose, be changed into ketone bones, etc. If you already have enough energy for the moment being, it will most likely be turned into acetyl-CoA and turned into fatty acids which then get packaged into triglycerides for storage. So i guess in excess, yes it will be stored as fat.
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Last edited by Confuzzl3dOn3; 09-03-2009 at 09:47 PM.
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09-04-2009, 12:23 AM
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#9
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Does I have catabolismz?
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1. Amino acids can be stored. There is an AA pool, albeit small, in the body for storage in muscle tissue. Not likely enough to provide a significant source of energy.
2. It is possible to build muscle on a calorie deficit, albeit slowly, if you are mobilizing bodyfat for energy and optimizing your body for anabolism. A fat-adapted individual, as one who has been on a keto diet for a significant period, is especially suited to this. It's known as "recomping", or the holy grail of body composition diets. Yes it's possible, no its not easy or fast, but keto makes it easier, IME, on a MODERATE calorie deficit. Go too high and you will screw yourself. period.
3. Nitrogen retention is not a broscience term, it refers to the in/out balance of nitrogenous compounds (read: protein) in the body. You want nitrogen retention because it indicates the body is in an anabolic state; it is consuming more nitrogen than it is excreting, aka net anabolism.
4. In a fat-adapted individual, the body will not turn as readily to muscle protein for energy. That individual has taught the body to run efficiently on fat. This will occur within reason if other parameters are optimal.
The problem many people have is they say "hey i iz going on keto, i eatz 250 g protein, 30 g or less carbz and 30 g fatz, does i have catabolismz?" YES, the body needs either adequate fat of adequate carbs for an energy source. You cannot eat a low-fat low-carb high-protein diet for long without consequences.
5. mtor is the mammalian target of rapamyacin. It has an interaction with leucine. This is a fascinating area currently being researched by str8flexed/Layne Norton. Basically, leucine has been identified as a primary AA responsible for signaling anabolism to the body. The anabolic response to a meal is dependent to a large extent on the leucine content of said meal. Lookup Layne's research for more explanation than I can give you here.
6. On that subject, BCAAs are unique in that they are metabolized not in the liver, but in muscle tissue. The thought is if you supply muscle tissue with enough BCAA, it will keep the body from breaking muscle down for energy. This is why BCAA is famed to have anti-catabolic properties.
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09-04-2009, 03:41 AM
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#10
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Quote:
Originally Posted by TaoistWarrior
1. Amino acids can be stored. There is an AA pool, albeit small, in the body for storage in muscle tissue. Not likely enough to provide a significant source of energy.
2. It is possible to build muscle on a calorie deficit, albeit slowly, if you are mobilizing bodyfat for energy and optimizing your body for anabolism. A fat-adapted individual, as one who has been on a keto diet for a significant period, is especially suited to this. It's known as "recomping", or the holy grail of body composition diets. Yes it's possible, no its not easy or fast, but keto makes it easier, IME, on a MODERATE calorie deficit. Go too high and you will screw yourself. period.
3. Nitrogen retention is not a broscience term, it refers to the in/out balance of nitrogenous compounds (read: protein) in the body. You want nitrogen retention because it indicates the body is in an anabolic state; it is consuming more nitrogen than it is excreting, aka net anabolism.
4. In a fat-adapted individual, the body will not turn as readily to muscle protein for energy. That individual has taught the body to run efficiently on fat. This will occur within reason if other parameters are optimal.
The problem many people have is they say "hey i iz going on keto, i eatz 250 g protein, 30 g or less carbz and 30 g fatz, does i have catabolismz?" YES, the body needs either adequate fat of adequate carbs for an energy source. You cannot eat a low-fat low-carb high-protein diet for long without consequences.
5. mtor is the mammalian target of rapamyacin. It has an interaction with leucine. This is a fascinating area currently being researched by str8flexed/Layne Norton. Basically, leucine has been identified as a primary AA responsible for signaling anabolism to the body. The anabolic response to a meal is dependent to a large extent on the leucine content of said meal. Lookup Layne's research for more explanation than I can give you here.
6. On that subject, BCAAs are unique in that they are metabolized not in the liver, but in muscle tissue. The thought is if you supply muscle tissue with enough BCAA, it will keep the body from breaking muscle down for energy. This is why BCAA is famed to have anti-catabolic properties.
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Awesome info! Thanks!
Number 6 is an interesting one, and really the one that prompted my original post.
I have read many people argue both sides of the supplemented BCAA being used as energy in the absence of glucose.
I know the Scivation guys swear that since BCAA (xtend) are not complete proteins, they have zero calories, and thereby cannot be used as energy or stored as fat. I believe the FDA also states this if I am not mistaken.
I have read several others state that xtend and BCAA supplements absolutely have calories and absolutely will be used as energy in a calorie deficit.
Logic would tell me that in ketosis, where fat has become the bodies primary fuel source instead of glucose, that BCAA's would not be used as energy, even if they could be, unless a person were to do more intense type exercising (over 120 HR), even in a caloric deficit.
Now, if someone were not in ketosis, yet in a caloric deficit, glucose is still the primary fuel source, and I would think in that case AA's and xtend type supplements are more likely to
get used as fuel since AA's can be easily converted to glucose (Gluconeogenesis).
Anyone have any thoughts/knowledge/links on the topic of BCAA's containing calories or not, and if they can be used as energy? Also, does my logic on the ketones vs glucose fuel source hold true?
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09-04-2009, 04:24 AM
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#11
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learn'n 2 EAT!LIFT!SLEEP!
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All i know, is that in initial starvation/caloric deficiency, i think the first 1-3 days, proteolysis of muscle is present but the amount depends on how sever the caloric deficit. Ketone body production is also present but proteolysis is still quite significant. I think after this early starvation period, proteolysis eases off and your body will switch into basically full keto mode and use fat for ketone bodies rather than turn your muscle protein to amino acids for gluconeogenesis. Hope that helps.
__________________
125lbs wtf!! Let's get down and dirty and fking bulk Rippetoe SS style!!
Follow my Rippetoe's SS workout program.
http://forum.bodybuilding.com/showthread.php?t=116623681
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09-04-2009, 05:09 AM
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#12
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Does I have catabolismz?
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Quote:
Originally Posted by Confuzzl3dOn3
All i know, is that in initial starvation/caloric deficiency, i think the first 1-3 days, proteolysis of muscle is present but the amount depends on how sever the caloric deficit. Ketone body production is also present but proteolysis is still quite significant. I think after this early starvation period, proteolysis eases off and your body will switch into basically full keto mode and use fat for ketone bodies rather than turn your muscle protein to amino acids for gluconeogenesis. Hope that helps.
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That's why it's a big mistake to switch to keto and go immediately into a calorie deficit. It's better to eat excess calories to ensure a successful switch before cutting the cals.
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09-04-2009, 03:32 PM
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#13
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You wrote a great post, but I wanted to address some of your points that touched on my original points...
Quote:
Originally Posted by TaoistWarrior
1. Amino acids can be stored. There is an AA pool, albeit small, in the body for storage in muscle tissue. Not likely enough to provide a significant source of energy.
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Technically speaking, one would never say that there is a storage of a.a's. What we have is a "pool" of a.a.s in the form of protein in muscle tissue. But we really don't store aas.
Quote:
Originally Posted by TaoistWarrior
3. Nitrogen retention is not a broscience term, it refers to the in/out balance of nitrogenous compounds (read: protein) in the body. You want nitrogen retention because it indicates the body is in an anabolic state; it is consuming more nitrogen than it is excreting, aka net anabolism.
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Sorry for the mis-characterization. Usually those terms come from the way that protein is assayed (nitrogen tests), but in reality a better name for it is amino acid retention, protein retention, etc.
Personally, I dislike the term... I have also heard of "nitrogen balance", same thing...
I am also sure that when this terms were coined, no one knew that Nitrogen itself is a signaling molecule...
Quote:
Originally Posted by TaoistWarrior
5. mtor is the mammalian target of rapamyacin. It has an interaction with leucine. This is a fascinating area currently being researched by str8flexed/Layne Norton. Basically, leucine has been identified as a primary AA responsible for signaling anabolism to the body. The anabolic response to a meal is dependent to a large extent on the leucine content of said meal. Lookup Layne's research for more explanation than I can give you here.
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mTOR has been the target of some serious research... Layne Norton is not the only one... Just wanted to clear that up...
I think that you are (on purpose?) oversimplifying the role of mTOR. Its much more complex than that, as it integrates signals from several pathways (including IGF-1, Growth Hormone, etc), and it is actually involved in muscle hypertrophy (specially its role in regulating satellite cells) and not just anabolism...
Quote:
Originally Posted by TaoistWarrior
6. On that subject, BCAAs are unique in that they are metabolized not in the liver, but in muscle tissue. The thought is if you supply muscle tissue with enough BCAA, it will keep the body from breaking muscle down for energy. This is why BCAA is famed to have anti-catabolic properties.
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They are also more insulogenic and (I believe) gluconeogenic. Because leucine is also an activator of mTOR, and leucine is a BCAA, the BCAAs have many ways of acting to promote muscle synthesis.
Great little article on BCAAs which mentions mTOR:
http://www.ajiaminoscience.com/pdf/a...mino_Acids.pdf
I have a great review of mTOR but its probably a bit dated now (perhaps is 2007 maybe 2008). I have to dig it out if anyone is interested...
However, wikipedia has a great little entry on it:
http://en.wikipedia.org/wiki/Mammali...t_of_rapamycin
Like you, I am also no expert on this subject. Layne Norton has some great articles on this. However, I really like the succinct explanation offered in wikipedia as to what mTOR is:
Quote:
Current research indicates that mTOR integrates the input from multiple upstream pathways, including insulin, growth factors (such as IGF-1 and IGF-2), and mitogens.[3] mTOR also functions as a sensor of cellular nutrient and energy levels and redox status.[5] The disregulation of the mTOR pathway is implicated as a contributing factor to various human disease processes, especially various types of cancer.[4] Rapamycin is a bacterial natural product that can inhibit mTOR through association with its intracellular receptor FKBP12.[6][7] The FKBP12-rapamycin complex binds directly to the FKBP12-Rapamycin Binding (FRB) domain of mTOR.[7]
[8]
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__________________
Dr. ReefPicker (PhD)
-Not a Dr. in Nutrition or any other Human Biology Field-
Fish Scientist / Computer Geek / Gymaholic
---------------------------------------------------------
Ovolactate Pescaterian and scientist.
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