Monday, March 13, 2006

Amino Acids/long


I and others keep hitting amino acids. Tryptophan, Arginine, etc.

So i saved some posts from others as to them. Enjoy eating meat?

Or the other foods containing them? What do they do?

I am sure that the prorialess site is bogus as if one used their products and diet. (eating meat= high tryptophan=bad for you) On this diet sure you would clear from no arachidonic acid from meat. But then you'd miss other essential amino acids that you've been getting from a balanced diet. So the psorialess folks trick you to think its tryptophan and that their products are the cure. I don't think so. /Sure maybe you eat to much meat protein. But to be a little heavy is better then thin. Right? Cept. for you who can never be to rich or thin-sters.

here goes... amino acids from people who use them for reasons...

***************** Alanine is a non-essential amino acid that is involved in the metabolism of tryptophan and the vitamin pyridoxine. The alpha-c! arbon in alanine is substituted with a levorotatory (l)-methyl group, making it one of the simpliest amino acids with respect to molecular structure. This amino acid is one of the most widely used in protein construction, averaging about 9 percent of average protein composition on a per-mole basis when compared with the other amino acids. Alanine has little therapeutic role in humans, although it has been demonstrated to display a cholesterol-reducing effect in rats.

This is the only naturally occuring beta amino acid, however this biochemical is not used in the biosynthesis of any major proteins or enzymes. Structurally, the IUPAC name for beta-alanine would be 3- (or beta- ) aminopropionic acid. It is a component of the naturally occuring peptides carnosine and anserine and also of pantothenic acid (vitamin B-3) which itself is a component of coenzyme A. Under normal conditions, beta-alanine is metabolized into acetic acid.

Arginine is a compl! ex amino acid that is often found at the active (or catalytic) site i n proteins and enzymes due to its amine-containing side chain. Although arginine is considered an essential amino acid (it must be obtained through the diet), this is true only during the juvenile period in humans. Arginine is incorporated in proteins at about a 4.7 percent on a per-mole basis when compared to the other amino acids. Natural sources of arginine are brown rice, nuts, popcorn, raisins, and whole-wheat products.

^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^ (Martin Banschbach, Ph.D.) writes:

Infection increases the need for many nutrients but arginine (ornithine) requirements seem to increase more than other nutrients.

I agree.  Protein malnutrition has long been known to increase infection suceptibility.  Protein plays many roles in the immune response but one of the most important is probably NO production.  Another area that I also think is very important is polyamine formation.  Both! processes reguire arginine (although polyamine formation also uses ornithine).

I too have had the same problem Michael.  Arginine and ornithine combinations do seem to improve muscle development.  The easiest explanation is to point the finger at growth hormone but as you point out, the IV dose is quite high compared to the oral dose that seems to be effective for many people.

Since muscle fiber formation requires all amino acids, a lack of adequate arginine could be limiting in muscle fiber formation (but the high protein intake for many body builders seems to make this unlikely).

Amino acid transamination is directly tied into the urea cycle. Without this cycle turning over rapidly, amino acid transamination is not going to procede at a normal rate and since transamination is used to form most of the nonessential amino acids, a sluggish urea cycle could impede muscle fiber development.  Using arginine and ornithine (which are! both intermediates in the urea cycle) could improve nonessential ami no acid formation and aid muscle fiber development.

Bodybuilders also often report that their muscle development is seriously affected by viral infections, even when the infection is not severe enough to keep them out of the gym.  During a virial infection, polyamine formation is greatly increased.  Ornithine and arginine are both used (consumed) to form putrescine which in term gets converted to spermidine and spermine using SAM.  During virial infections polyamine systhesis increases and the increased polyamines bind to DNA where they are believed to help stabilize it and prevent virial insertion of genetic material into eukaryotic DNA.  If we also have increased NO formation, the requirement for arginine could easily exceed dietary and urea cycle capabilities unless supplemental arginine (ornithine) is used.  This increased need for both arginine and ornithine could very easily impair muscle fiber formation (fighting the i! nfection is much more important than building muscle fibers).

One other area where arginine and ornthine may be involved in muscle development is seminal fluid formation.  Atheletes have often been encouraged to not release their sperm while in training (no sex). Seminal fluid has the highest concentraion of polyamines of any tissue (fluid) in the human body.  If you are dumping these polyamines on a regular basis, you may impair muscle development if you are not using arginine and ornithine supplements.

I'm not into bodybuilding or any kind of training program but if my trainer or coach told me to refrain from sex, I'd just use ornithine and arginine and continue to place those polyamines into my sex partner.


The strain on organs are those involved with handling excess nitrogen. It's the nitrogen of protein that needs to be eliminated. The remaining carbon chains can be recycled into either fat or carbs. !

To eliminate the nitrogen, the liver performs the urea cycle. Nit rogen on arginine and its derivatives are converted into urea (a small molecule with a high percentage of nitrogen). I've speculated in the past that the supposed benefits of arginine supplementation (alleged to be due to growth hormone induction which is not physiologically relevant) might be because of improvement in handling higher protein turnover and increased intake by increasing the throughput of the urea cycle.

Urea is then excreted by the kidneys. The kidneys can also utilize nitrogen for excretion by producing ammonia (NH3) for use as a pH buffer when alot of acid is excreted.

The adverse effects of nitrogen on kidney function are due to evidence in human with pre-existing kidney disease that high protein diets accelerate progression of the disease and low protein diets prolong kidney functioning. There are also rat studies suggesting that high protein diets with normal kidneys leads to kidney disease.

The original (and I believe current) W! HO recommendations call for 0.8 g per kilogram of bodyweight per day. This number is for a sedentary individual. What little data there is out there suggests that exercising individuals probably need at least 1.5 g per kg per d.

For those who question the need for extra protein requirement for active individuals, even the WHO figures detail increased protein requirements for increasing daily energy expenditures. Since resting metabolism is not going to change that much, the extra energy expenditure has to come in the form of physical activity. Increasing physical activity increases protein requirements.


Asparagine, the beta-amido derivative of aspartic acid, is considered a non-essential amino acid. This amino acid plays an important role in the biosynthesis of glycoproteins and is also essential to the synthesis of a large number of other proteins. On a per-mole basis, asparagine is incorporated into proteins and enzymes at a! rate of 4.4 percent with respect to the other amino acids.

Aspa rtic acid is one of two amino acids (the other is glutamic acid) that has a negatively charged carboxylate group on the side chain. This gives aspartic acid an overall negative charge at physiological hydrogen ion concentrations (approximately pH 7.3). Although aspartic acid is considered a non-essential amino acid, it plays a paramount role in metabolism during construction of other amino acids and biochemicals in the citric acid cycle. Among the biochemicals that are synthesized from aspartic acid are asparagine, arginine, lysine, methionine, threonine, isoleucine, and several nucleotides.

The major biochemical function of carnitine is to act as a trans-membrane carrier of fatty acids to the interior of mitochondria. Carnitine is not used in the biosysnthesis of proteins or enzymes and has an unusual structure compared to the classical amino acids. It is synthesized naturally from the amino acids methionine and lysine, but good external sources of carnitine are milk products and meats.

Citrulline exists primarily in the liver, where it is heavily involved in the urea cycle to detoxify and excrete ammonia. This unusual amino acid is formed in the urea cycle by the addition of carbon dioxide and ammonia to ornithine. Next, it is combined with aspartic acid to form arginosuccinic acid, which later is metabolized into the amino acid arginine. Citrulline is not a component of any major proteins or enzymes.

  Amino acids are very small biomolecules with an average molecular weight of about 135 daltons. These organic acids exist naturally in a zwitterion state where the carboxylic acid moiety is ionized and the basic amino group is protonated. The entire class of am! ino acids has a common backbone of  an organic carboxylic acid group and an amino group attached to a       saturated carbon atom. The simplest member of this group is glycine, where  the saturated carbon atom is unsubstituted, rendering it optically inactive.

  The rest of the 20 most common amino acids are optically active existing as  both D and L stereoisomers. Naturally occuring amino acids that are incorporated into proteins are, for the most part, the levorotary (L) isomer.  Substituents on the alpha (or saturated) carbon atom vary from lower alkyl groups to aromatic amines and alcohols. There are also acidic and basic  side chains as well as thiol chains that can be oxidized to dithiol linkages between two similar amino acids

  Amino acids are the principal building blocks of proteins and enzymes. They  are incorporated into proteins by transer RNA according to the genetic code while messenger RNA is being decoded by ribosomes. During and after the fi! nal assembly of a protein, the amino acid content dictates the spatial and biochemical properties of the protein or enzyme.

  The amino acid backbone determines the primary sequence of a protein, but the nature of the side chains determines the protein's properties. Amino acid  side chains can be either polar, non-polar, or practically neutral. Polar side  chains tend to be present on the surface of a protein where they can interact  with the aqueous environment found in cells. On the other hand, non-polar  amino acids tend to reside within the center of the protein where they can  interact with similar non-polar neighbors. This can create a hydrophobic  region within an enzyme where chemical reactions can be conducted in a  non-polar atmosphere. Likewise, enzymes can also have polar amino acid  substituents within the active site that provide a polar region in which to  conduct biochemical synthesis.!

  Alanine -- The second most simple amino acid, but used the most in proteins.  beta-Alanine -- The only naturally occuring beta amino acid. Arginine -- Amino acid often used at the active sites of enzymes. Asparagine -- Amide derivative of aspartic acid.  Aspartic Acid -- Important intermediate in the citric acid cycle.  Carnitine -- Unusual amino acid that carries fatty acids into mitochonria.  Citrulline -- An amino acid that works to detoxify and eliminate unwanted  ammonia.  Cysteine -- Thiol containing amino acid involved in active sites and protein tertiary  structure determination.  Cystine -- Oxidation product of cysteine that holds proteins together.  gamma-Aminobutryic Acid -- Decarboxylated amino acid that helps you chill  out.  Glutamic Acid -- Negatively charged amino acid found on the surface of proteins.  Glutathione -- Small peptide that helps dump free radicals.  Glycine -- Simplest amino acid that also acts as a neurotransmitter ! antagonist.  Histidine -- Amino acid responsible for histamine biosynthesis.  Hydroxyproline -- Important amino acid used in structural proteins like collagen.  Isoleucine -- Hydrophobic amino acid used almost exclusively in protein and  enzyme construction.  Leucine -- Another hydrophobic amino acid used almost exclusively in protein  and enzyme construction.  Lysine -- An essential amino acid with a positive charge. Methionine -- An essential amino acid that helps initiate protein synthesis. Ornithine -- Critical member of the amino acids in the urea cycle. Phenylalanine -- Most common aromatic amino acid found in proteins. Proline -- Cyclic aliphatic amino acid used in the synthesis of collagen. Serine -- Amino acid alcohol found in the active site of serine proteases. Taurine -- Mercaptin-containing amino acid that is involved in bile acid biochemistry. Threonine -- Amino acid alcohol involved in porphyrin metaboli! sm. Tryptophan -- Aromatic amino acid used the least frequently in p roteins. Tyrosine -- Hydroxyphenyl amino acid that is used to build neurotransmitters  and hormones.  Valine -- Hydrophobic aliphatic amino acid used to hold proteins together.


include detection for two other enzyme deficiencies in the same family as my son's enzyme deficiency and these are nearly as lethal as my son's specific affliction. My son's metabolic system (liver, kidney and colon) lacks the gene required for production of ornithine transcarbamylase (OTC), which is part of the urea cycle in protein metabolism. As everyone probably knows, protein contains nitrogen molecules, which are made up of atoms that include ammonia atoms. The urea cycle in our bodies functions to remove ammonia atoms from the nitrogen molecules and send them out of our bodies via our waste. This is why if you may have noticed the smell of ammonia where a person or animal has urinated.

There are five steps in the urea cycle, e! ach providing a different enzyme that removes a different ammonia atom. If any of those steps are missed, ammonia atoms escape back into the body's bloodstream and eventually accumulate to the point of poisoning the suffer's brain. OTC is the second stage of the cycle and removes the greatest amount of ammonia from protein. OTC deficiency is the most prevalent of the urea cycle disorders because, unlike the others, it's an X-linked trait, meaning it is passed on by a mother carrier. The other four deficiencies are all recessive, meaning both parents must carry the recessive gene for the disorder before a child can be affected. Because only one parent is required to pass on OTC def, it's obviously "easier" to get (estimated at 1 in 75,000 live births). Boys are especially hard hit, since they don't have another X chromosome, as do girls, to compensate. I am a carrier, but have no symptoms because my other "non-impaired" X chromosome! provides enough of the enzyme for me to metabolize normally. My poor little boy has a complete deficiency and it nearly killed him. A liver transplant at age 6 mos effectively "cured" him of the disorder. That's the good news....but we're living always w/ the brain damage because there was no screening available, as there is for PKU, when he was born.

There still is no screening available for OTC deficiency because OTC is not a stable property and it can't be tested for in newborns reliably; but this $25 test does screen for two other deficiencies in the same cycle. These two are not as deadly as quickly as my son's enzyme deficiency is, but they can be just as bad eventually, if not treated properly.


Oh, i figured a disease may help to put the amino's in perspective.

randall.... all from eating some meat. Of course fats are good and bad. Next?


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