60 Vegi-Caps
AOR04196
750mg
100% Vegetarian

Suggested Use
Take two capsules daily with or without food, or as directed by a qualified health care practitioner.

Main Applications
• Supports proper metabolism and energy production 
• Cardiovascular health

Source
Pharmaceutical Synthesis

Pregnancy / Nursing
Do not use if pregnant or nursing.

Cautions
None Known

*These statements have not been evaluated by the Food and Drug Administration. This product is not intended to diagnose, treat, cure, or prevent any disease.

60 Vegi-Caps
AOR04196
750mg
100% Vegetarian

Suggested Use
Take two capsules daily with or without food, or as directed by a qualified health care practitioner.

Main Applications
• Supports proper metabolism and energy production 
• Cardiovascular health

Source
Pharmaceutical Synthesis

Pregnancy / Nursing
Do not use if pregnant or nursing.

Cautions
None Known

*These statements have not been evaluated by the Food and Drug Administration. This product is not intended to diagnose, treat, cure, or prevent any disease.

60 Vegi-Caps
AOR04196
750mg
100% Vegetarian

Suggested Use
Take two capsules daily with or without food, or as directed by a qualified health care practitioner.

Main Applications
• Supports proper metabolism and energy production 
• Cardiovascular health

Source
Pharmaceutical Synthesis

Pregnancy / Nursing
Do not use if pregnant or nursing.

Cautions
None Known

*These statements have not been evaluated by the Food and Drug Administration. This product is not intended to diagnose, treat, cure, or prevent any disease.

Butyrobetaine is equal to L-carnitine in elevating L-carnitine levels in rats
Sandor A. Biochim Biophys Acta. 1991 May 8;1083(2):135-8.
This work shows that butyrobetaine administered to rats in a single dose can be highly effective in elevating L-carnitine levels in all tissues. This ability of butyrobetaine was compared to that of L-carnitine. In an experiment with tracer dose of the compounds, 12 h following administration of [3H]butyrobetaine plasma and tissues contained radioactivity exclusively in L-carnitine and in similar amounts as in the other group of animals receiving L-[3H]carnitine. This was observed both after intraperitoneal and oral administration of the compounds. In the loading experiments 100 mumol [3H]butyrobetaine was administered orally to one group and 100 mumol L-[3H]carnitine to the other group of animals and 12 h later it was found that butyrobetaine caused the same increments in L-carnitine as L-carnitine administration. The increments in the organs of the butyrobetaine-treated group (in decreasing order) were as follows: kidney, 1227 nmol/g vs. 652 nmol/g; liver, 469 nmol/g vs. 258 nmol/g; muscle, 1043 nmol/g vs. 881 nmol/g; plasma, 79.4 nmol/ml vs. 39.3 nmol/ml. Butyrobetaine (100 mumol) caused similar increments when it was administered intraperitoneally. Based on these results butyrobetaine can be considered as a potential agent for L-carnitine supplementation therapy.

gamma-Butyrobetaine hydroxylase activity is not rate limiting for carnitine biosynthesis in the human infant
Olson AL, Rebouche CJ. J Nutr. 1987 Jun;117(6):1024-31.
Carnitine biosynthesis was assessed in human infants by measuring changes in plasma carnitine concentration and rates of urinary carnitine excretion after infants were fed carnitine-free formulas with and without added e-N-trimethyl-L-lysine or gamma-butyrobetaine. This study was undertaken to test the hypothesis that carnitine biosynthesis in the human infant is regulated by substrate availability rather than activity of gamma-butyrobetaine hydroxylase, the final enzyme in the carnitine biosynthetic pathway. Ten infants were fed carnitine-free formula supplemented with either 500 µM e-N-trimethyl-L-lysine or 500 µM gamma-butyrobetaine for 14 d. Plasma carnitine concentration and rate of urinary carnitine excretion were measured in infants before and after this period. Plasma carnitine concentration increased twofold when infants were fed gamma-N-trimethyl-L-lysine and increased threefold when infants were fed gamma-butyrobetaine. The rate of carnitine excretion doubled when infants were fed -N-trimethyl-L-lysine and increased 30-fold when infants were fed gamma-butyrobetaine. Absorption of e-N-trimethyl-L-lysine was verified by demonstrating increased urinary excretion of e-N-trimethyl-L-lysine in infants fed this substrate. We conclude that gamma-butyrobetaine hydroxylase activity is not rate limiting for carnitine biosynthesis in the human infant. Development of renal and hepatic gamma-butyrobetaine hydroxylase activity was determined in necropsy tissue from individuals of various ages. It was verified that gamma-butyrobetaine hydroxylase activity is developmentally regulated in the liver, but not in the kidney. The clinical relevance of this observation is diminished in view of the results of the in vivo studies of carnitine biosynthesis in infants.

Utilization of dietary precursors for carnitine synthesis in human adults
Rebouche CJ, Bosch EP, Chenard CA, Schabold KJ, Nelson SE. J Nutr. 1989 Dec;119(12):1907-13.
Endogenous synthetic pathways are presumed to be sufficient to provide adequate amounts of carnitine to meet the needs of the body. However, circulating carnitine levels of strict vegetarian adults and children, and particularly of infants fed carnitine-free formulas, are significantly lower than normal. Therefore, we investigated loci at which rates of carnitine synthesis may be restricted in human adults. Excess amounts of the carnitine precursors lysine plus methionine, e-N-trimethyllysine or gamma-butyrobetaine were fed as supplements to a low carnitine diet for 10 d. Rate of carnitine synthesis was estimated by changes in carnitine excretion and changes in serum and muscle carnitine levels. Dietary gamma-butyrobetaine dramatically increased camitine production, e-N-trimethyllysine had a somewhat smaller effect, and lysine plus methionine had even less effect on carnitine synthesis. We conclude that carnitine synthesis is not limited by the activity of gamma-butyrobetaine hydroxylase. Carnitine synthesis from exogenous e-N-trimethyllysine is limited either by enzymatic processes that lead to the final intermediate, gamma-butyrobetaine, or by the ability of this substrate to enter tissues capable of carrying out these transformations.

L-carnitine Monograph
Altern Med Rev. 2005 Mar;10(1):42-50.
A trimethylated amino acid, roughly similar in structure to choline, L-carnitine is a cofactor required for transformation of free long-chain fatty acids into acylcarnitines, and for their subsequent transport into the mitochondrial matrix, where they undergo beta-oxidation for cellular energy production. Conditions that appear to benefit from exogenous supplementation of L-carnitine include anorexia, chronic fatigue, cardiovascular disease, diphtheria, hypoglycemia, male infertility, muscular my-opathies, and Rett syndrome. Preterm infants, dialysis patients, and HIV-positive individuals seem to be prone to a deficiency of L-carnitine and benefit from supplementation. Although discovered in 1905, the crucial role of L-carnitine in metabolism was not elucidated until 1955, and its deficiency was not described until 1972. The most significant source of L-carnitine in human nutrition is meat, although humans can synthesize L-carnitine from dietary amino acids.