The Active Methionine
What is S-Adenosyl Methionine (SAM-e)?
S-Adenosyl Methionine (S-adenosyl-L-methionine or SAM-e) is an amino acid derivative that has been clinically proven to benefit brain, liver, and joint function . Found in all living cells, SAM-e is also called "activated methionine" (an essential amino acid) since it is formed by the combination of ATP (adenosine triphosphate) and methionine. Simply supplementing with methionine, however, does not result in SAM-e elevation: conversely, methionine can cause elevation of the toxic amino acid homocysteine. SAM-e has undergone dozens of clinical trials involving thousands of patients. Researchers studying the beneficial efforts of SAM-e have identified many structure and function-based benefits of SAM-e.
Liver Detoxification
SAM-e metabolism supports the synthesis of glutathione (GSH) and glutathione-dependent enzymes (glutathione peroxidase and glutathione-S-transferase), which are important for liver function.
Glutathione is necessary for scavenging free radicals produced by glycolysis, the breakdown of carbohydrates for energy. The amino acid taurine is another end product of SAM-e metabolism. The glutathione family of compounds and taurine are important for liver detoxification reactions.
Brain Function
SAM-e supports brain function by its methylation effects. Methylation is the process by which a four atom appendage know as methyl group (unit of one carbon and three hydrogen atoms) is transferred from one molecule to another. Of all methyl-donating substances known in mammalian metabolism, SAM-e is the most important.
The donation of methyl groups affects proper function of many metabolic processes including brain function, energy production and DNA metabolism. Neurotransmitters, substances involved in the brain's cell-to-cell communication, are the products of substances known in mammalian methylation reactions. These compounds include L-dopa, dopamine, epinephrine and phosphatidylcholine (a component of lecithin).
Energy Production
Methylation from SAM-e is critical for proper energy production as it coverts guanidinoacetate to creatine. Creatine metabolizes to creatine phosphate, which is important for recycling of ADP to ATP. Creatine maximizes physical performance, reduces exercise fatigue and improves recovery after exercise.
Longevity
Methylation of DNA appears to be important in the prevention of DNA imperfections. The demethylation of DNA is considered to contribute to the aging process. Proper methylation through substances such as SAM-e positively influence longevity.
Not All SAM-e is Created Equal Jarrow Formulas® SAM-e is of the active (S,S) form. SAM-e is a chiral molecule and therefore consists of two forms: (S,S) SAM-e and (R,S) SAM-e. The biologically active form is the (S,S) structure, while the (R,S) structure is a biologically inactive. Jarrow Formulas® SAM-e is made naturally by microbiological fermentation and then specially processed, without solvents, to preserve 68-80% (S,S) SAM-e, the highest active level available.
Because SAM-e is a highly reactive molecule, it is very fragile. It degrades rapidly under conditions of high heat and/or humidity. Improper handling of SAM-e can cause its degradation in a matter of hours, resulting in a loss of biological activity. This is why the manufacturing process for Jarrow Formulas® SAM-e is done under low temperature and low humidity, and the tablet is enteric coated and blister-packed.
Pharmacokinetic studies show that oral supplementation of SAM-e is most effective when enteric-coated by special gastric fluid-resistant polymers. Enteric coating SAM-e results in maximum SAM-e levels in the bloodstream.
Source: Jarrow Formulas
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Scientific References
- Murray, RK, et al., (1996) Harper's Biochemistry (24th edition). (Standford, CT: Appleton & Lange.
- Strementinoil, (1987) Pharmacologic Aspects of S-adenosyl-methionine: Pharmacokinetics and Pharmacodynamics, American Journal Of Medicine 83, Suppl. 5A, 35-42.
- McCully, Kilmer S., The Homocysteine Revolution. (New Canaan, CT: Keats Publishing, Inc., 1997)
- Frankel, Paul and Madsen, Fred, Stop Homocysteine Through the Methylation Process. (Thousands Oaks, CA: The Research Corner, 1988).
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