C-Reactive Protein, a Known Risk Factor

C-reactive protein, abbreviated CRP, is produced in the liver and released into the bloodstream when there is inflammation in the body.[1] It can be measured in the blood, and is a known risk factor for many common diseases. Unfortunately, the blood test does not pinpoint where the inflammation is coming from or what is causing it.

Research shows that people with high CRP concentrations are more likely to develop heart attacks, strokes and severe peripheral vascular disease.[2]   Research also shows that people with elevated levels of CRP are at an increased risk of diabetes.[3][4]

An elevated level of CRP can be observed in people with inflammatory bowel diseases such as ulcerative colitis and Crohn’s disease.[5]

The normal concentration of CRP in a healthy person’s blood serum is usually lower than 10 mg/L. This number increases slightly with aging. Levels of 10–40 mg/L are found in women during late pregnancy and in people with mild inflammation and viral infections. Active inflammation and bacterial infection bring the level up from 40–200 mg/L. Severe bacterial infections and burns may bring the level to greater than 200 mg/L.[6]

Fortunately for us, it is possible to lower CRP. There are both, natural methods and pharmaceutical drugs that will the job. However, I suggest the natural approach because anti-inflammatory drugs are known to have many unhealthy side effects. The natural approach usually yields positive effects such as increased vitality.

Diet plays a major role in the elevation of CRP. A study was done on over 700 nurses. They split the group into four segments. Those in the group with the highest trans-fat consumption had blood levels of CRP that were 73% higher than those in the group with the lowest trans-fat consumption.[7]  Saturated fats have also been shown to raise CRP.

Hidden food allergies are a common cause of elevated levels of CRP.  Foods to avoid include refined glutinous flour products, refined sugars and processed food.

Bacterial infections, viral infections, obesity, stress, cigarette smoking, lack of exercise, toxins such as heavy metals, pesticides [8] and mold spores have also been associated with elevated levels of CRP.

There are healthy nutritional supplements that have been shown to lower CRP. Omega 3 fats are highly anti-inflammatory. The cleanest source of omega 3 is DHA from algae oil.

You can also add turmeric to your diet. In Italy, there was a three-month trial with 50 people. A team of researchers were investigating the effect of treating people who had arthritis with an oral turmeric extract called curcumin.  After 90 days, blood tests showed a 16-fold decline in C-reactive protein levels.[9]

To sum it up, I suggest the consumption of a plant based diet composed primarily of unprocessed whole food, avoiding the unhealthy fats and the common allergenic foods, gentle but regular exercise and the practice of stress reduction techniques.

Regardless of how you feel, studies show that it is important for everyone to be sure that their CRP level is not elevated. Many researchers now believe that knowing your CRP level is more important than knowing your cholesterol level.

[1] Pepys MB, Hirschfield GM (June 2003). "C-reactive protein: a critical update". J. Clin. Invest. 111 (12): 1805–12. doi:10.1172/JCI18921.PMC 161431PMID 12813013.

[2]- Clearfield MB (September 2005). "C-reactive protein: a new risk assessment tool for cardiovascular disease". The Journal of the American Osteopathic Association 105 (9): 409–16. PMID 16239491.

[3] Pradhan AD, Manson JE, Rifai N, Buring JE, Ridker PM (July 2001). "C-reactive protein, interleukin 6, and risk of developing type 2 diabetes mellitus".JAMA 286 (3): 327–34. doi:10.1001/jama.286.3.327. PMID 11466099.

[4] Dehghan A, Kardys I, de Maat MP, Uitterlinden AG, Sijbrands EJ, Bootsma AH, Stijnen T, Hofman A, Schram MT, Witteman JC (March 2007). "Genetic variation, C-reactive protein levels, and incidence of diabetes". Diabetes 56(3): 872–8. doi:10.2337/db06-0922. PMID 17327459.

 [5]-Liu S, Ren J, Xia Q, Wu X, Han G, Ren H, Yan D, Wang G, Gu G, Li J (May 2013). "Preliminary Case-control Study to Evaluate Diagnostic Values of C-Reactive Protein and Erythrocyte Sedimentation Rate in Differentiating Active Crohn's Disease From Intestinal Lymphoma, Intestinal Tuberculosis and Behcet's Syndrome". Am. J. Med. Sci. 346 (6): 467–72.doi:10.1097/MAJ.0b013e3182959a18.PMID 23689052

[6] Clyne B, Olshaker JS (1999). "The C-reactive protein". J Emerg Med 17 (6): 1019–25. doi:10.1016/S0736-4679(99)00135-3. PMID 10595891.

[7]  Lopez-Garcia E, Schulze MB, Meigs JB, Manson JE, Rifai N, Stampfer MJ, Willett WC, Hu FB (March 2005). "Consumption of trans fatty acids is related to plasma biomarkers of inflammation and endothelial dysfunction". J. Nutr.135 (3): 562–6. PMID 15735094.

[8] http://www.ncbi.nlm.nih.gov/pubmed/22509446

[9] http://www.ncbi.nlm.nih.gov/pubmed/20657536

 

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Acid Reflux, Treat the Cause, Not the Symptoms

Stomach acid is essential for good digestion and absorption of nutrients from your diet. Suppressing stomach acid only treats the symptoms, it does not treat the cause of the disease. In fact, it can actually make things worse. Taking acid blocking drugs long enough will cause numerous nutrient deficiencies, including vitamin, mineral, and especially vitamin B12 and amino acid deficiencies.

Studies have shown that people who take acid blocking drugs long term, may end up with a variety of illnesses including osteoporosis, hip fracture, IBS, fatigue, nerve damage and eventually dementia. Long term use can also lead to an overgrowth of clostridia in the small intestine that can be life threatening.

Stomach acid, also called hydrochloric acid (HCL) is needed for both, separating vitamin B12 from food to make it absorbable and also for breaking down protein rich food so that the amino acids can be absorbed. Not enough amino acids can lead to depression, insomnia, brain fog, anxiety, trouble building and maintaining muscles and more. Amino acids are precursors for essential neurotransmitters which are needed for proper brain function.

Stomach acid is essential for killing bacteria and other pathogenic organisms that might be ingested while eating or drinking. If the stomach acid is too low, these pathogens can colonize in your intestines and cause many health problems.

When pathogenic organisms take up residence in your digestive tract, they can create gas and bloating while feeding on the food you have eaten. The pressure from the gas and bloating can push up through the stomach and then through the upper stomach valve (esophageal sphincter) causing acid reflux.

A urine test or breath test for small bowel bacterial overgrowth can diagnose the presence of certain strains of bacteria.

Hiatal hernia can also cause acid reflux. This can be diagnosed with an x-ray. Extra fat around the midline can also contribute. Stress is another contributing factor.

Food allergies to gluten and dairy products may also contribute to acid reflux. I suggest completely eliminating these two foods for a month or so and see if it makes a difference. Other food allergies may also be a factor.

Nutritional deficiencies can also lead to acid reflux. If you are on a low sodium diet you might become deficient in the minerals sodium and chloride. Zinc, magnesium, vitamin C and B vitamins are also needed to have a properly functioning stomach.

Helicobacter pylori, is another common cause of acid reflux. However, unless you go to a holistic or functional medicine doctor, you most likely will not get tested for it unless you have an ulcer. H-pylori can be diagnosed with a simple stool test.

Numerous holistic and functional medicine doctors have been testing their clients who have acid reflux and finding that most of them have low stomach acid levels. Not high levels!

The following is an example of how low stomach acid can lead to acid reflux.

When the acid level in the stomach is too low, the upper stomach valve might not stay closed and the acid from the stomach can leak up into the throat. Our body needs to sense enough HCL in the stomach in order for the upper valve to stay closed properly. Note that in this case, acid reflux is caused by low stomach acid and not by high stomach acid. It is very often the case that people identify acid reflux as having too much stomach acid while most of the time it is caused by not enough stomach acid.

 

Traditional medical doctors are trained to prescribe acid blocking drugs to treat the symptoms and seem to overlook the dangers of using these drugs. Instead they should be testing the person’s stomach acid level, testing for microbial overgrowth or looking for other causes.

The gastric analysis by radio telemetry test is the most accurate way to measure stomach acid. One just needs to swallow a small capsule with a radio transmitter that measures the pH of the stomach. The result of this test provides you with a graph showing your pH levels at regular intervals over time. If the test shows the HCL level to be low, a betaine HCL supplement can be taken with meals to raise the acid which may keep the upper valve closed when food is present.

There are also two other tests. These can be done at home but are not very accurate. The baking soda test is performed by drinking ¼ teaspoon of baking soda mixed into 5 ounces of water first thing in the morning after waking up. Because the baking soda is very alkaline and your stomach should be very acidic, it will produce carbon dioxide gas that causes burping. You need to measure the exact amount of time that passes from the time you drink the solution until the time that the burping starts. The result gives you an idea of the amount of HCL in the stomach. If it takes more than five minutes to start burping, in may mean that you have low stomach acid. Please note that this test is not always accurate because there are many variables that can give false results.

The betaine HCL test for low stomach acid is the most reliable at home test you can perform. The test is done by taking a betaine HCL pill in the middle of a protein rich meal. If there is no burning sensation after the meal, then do the same thing at your next protein rich meal. If you do this several times and there is no burning sensation, most likely you have low stomach acid.

You may then take 2 pills in the middle of your next protein rich meal and wait to see if there is a burning sensation. Again, if there is no sensation, do the same thing at your next protein rich meal. You can raise the amount of pills by one after every few protein rich meals and see how many pills it takes to feel the burning sensation. When you finally get to the point that you feel the burning, you should then take one less pill during the next meal.

Now that you have determined how many pills your body needs, continue to supplement the HCL with protein rich meals. Over time, your body should need less and less of the HCL supplements as your stomach acid levels normalize. Eventually, you should be able to go off the supplement and not have reflux if the reflux was caused by low stomach acid.

If you have acid reflux, no matter what the cause, it is important to avoid overeating. You will also need to avoid acidic food items such as tomato sauce, fried food, soda, coffee, alcoholic beverages, spicy food and citrus. It is also very important to not eat for a few hours before lying down.

I suggest working with a qualified practitioner who can help you find the cause of the reflux and then slowly wean you off acid blocking drugs. Quitting acid blocking drugs can be dangerous if not supervised by an experienced doctor.

And last thing I would like to share is that there are nutritional supplements that can help. Probiotics are essential to colonize the intestines with good bacteria. DGL (deglycerized licorice) can help with the symptoms. Magnesium is an important nutrient for the proper function of the valves at the top and bottom of the stomach. These valves are actually muscles and muscles need magnesium. And a high quality multivitamin and protein supplement will help replenish nutritional deficiencies that were caused by the acid blocking drugs.

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How to Grow Strong Healthy Nails

Our nails can reflect our general state of health. No one wants to have weak brittle nails. Yet having brittle nails, also known as onychorrhexis, is a very common condition affecting approximately 20 percent of the population and is more common in women.[1]

Human fingernails and toenails are primarily composed of a protein called keratin and also contain an array of minerals. Keratin is an extremely strong protein.

Like other proteins, keratin is composed of amino acids. Keratin has large amounts of the sulfur-containing amino acid cysteine. Cysteine is required for giving nails their strength and rigidity.[2]

The mineral composition of a human nail includes: calcium, copper, iron, magnesium, sodium, sulphur and zinc. A deficiency in any one of these minerals can affect the health and growth of our nails.[3]

Aside from having a deficiency in the building blocks of nails, brittle nails can be caused by a variety of different things some of which include: chronic dehydration, a deficiency in omega-3 fatty acids and a biotin deficiency. [4]

Several chronic health conditions can also cause brittle nails, including: anorexia, bulimia, iron deficiency anemia, and underactive thyroid.[5] Furthermore, psoriasis has been linked to brittle nails. Brittle nails can even be a side effect of certain pharmaceutical medications.

And let’s not overlook the fact that nails which are excessively exposed to water, soap or solvents can also become brittle.

If you are wondering why some of your nails grow slower than the rest, there is no need to worry. In humans, the nail of the index finger may grow faster than that of the little finger and fingernails may grow up to four times faster than toenails.[6]

Provided you do not have a medical condition, keeping well-nourished with all the building blocks that nails need can result in strong healthy nails. A balanced diet composed primarily of a variety of unprocessed whole food is a great start.

To take your nails to the next level try supplementing your diet with a high quality protein powder, a good multi mineral complex, biotin and omega-3 fatty acids.

[1] Rapini, Ronald P.; Bolognia, Jean L.; Jorizzo, Joseph L. (2007). Dermatology: 2-Volume Set. St. Louis: Mosby. ISBN 1-4160-2999-0

[2] http://www.wisegeek.org/what-is-keratin.htm

[3] https://www.ncbi.nlm.nih.gov/pubmed/20620759  

[4] http://www.ncbi.nlm.nih.gov/pubmed/8477615

[5[ James, William; Berger, Timothy; Elston, Dirk (2005). Andrews' Diseases of the Skin: Clinical Dermatology. (10th ed.). Saunders. ISBN 0-7216-2921-0

[6]  Ravosa, Matthew J.; Dagosto, Marian (2007). Primate origins: adaptations and evolution. Springer. pp. 389–90. ISBN 0-387-30335-9
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Ten Reasons to Choose Plant Protein Over Whey Protein

  1. Whey protein linked to cancer promotion:

The hormone IGF-1 only occurs in animal protein, one of the best sources being protein from cow’s milk. IGF-1 has been shown to promote cancer cell growth in humans.[1]  Studies show that increased levels of IGF-1 lead to increased growth of existing cancer cells.[1] Dietary interventions and modifications such as vegan diets have been shown to down regulate (make less of) IGF-1 and have been associated with lower risk of cancer.[2]  It has been proven that people with exceptionally low levels of IGF-1 (Laron syndrome) are resistant to cancer.[3][4][5][6]   IGF-1 does not occur in plant protein and plant protein has not been shown to promote cancer growth.

  1. Whey protein linked to aggravation of acne:

According to studies, healthy male adults may develop acne after the consumption of whey protein. The studies indicate that dairy protein enhances IGF-1 and acne aggravation.[7][8] Plant protein has not been linked to acne.

  1. Whey protein linked to flatulence, bloating, cramps, diarrhea, nausea and rumbling stomach:

Seventy-five percent of all African American, Jewish, Mexican American, and Native American adults are lactose intolerant.[9] Both whey concentrate and whey isolate contain lactose.[10]  However, whey concentrates contain higher amounts of lactose.  Lactose intolerant people will suffer a variety of digestive issues which may include abdominal bloating, cramps, flatulence, diarrhea, nausea, vomiting and a rumbling stomach.[11]   Lactose only occurs in dairy protein and does not occur in plant protein.

  1. Whey protein may cause constipation:

Numerous studies concluded that constipation in children can have an allergic pathogenesis to whey and other dairy proteins.[12][13][14] Plant protein has not been linked to constipation.

  1. Whey protein can dangerously lower blood sugar:

Whey protein has been shown to lower blood sugar.[15] Caution is advised for people with diabetes or low blood sugar and in those taking drugs that affect blood sugar. According to Mayo Clinic, blood sugar levels may need to be monitored by a qualified healthcare professional and medication adjustments may be necessary for those consuming whey protein.[16] Plant protein has not been shown to have effects on blood sugar.

  1. Whey protein may cause abnormal heart rhythms:

According to Mayo Clinic, whey protein may cause abnormal heart rhythms.[16]  Plant protein has not been shown to effect heart rhythms.

  1. Whey protein may cause headaches:

According to Mayo Clinic, whey protein may cause headaches. [16] Plant protein has not been linked to headaches.

  1. Whey protein may increase the risk of diabetes:

According to Mayo Clinic, whey protein may increase the risk of diabetes. [16] Plant protein has not been linked to increased risk of diabetes.

  1. Whey protein may increase the risk of bleeding:

According to Mayo Clinic, whey protein may increase the risk of bleeding.[16] Caution is advised in people with bleeding disorders or in those taking drugs that may increase the risk of bleeding. Dosing adjustments may be necessary. Plant protein has not been shown to increase the risk of bleeding.

  1. Whey protein may cause drowsiness:

According to Mayo Clinic, drowsiness or sedation may occur when consuming whey protein. They advise using caution if driving or operating heavy machinery. Plant protein has not been linked to drowsiness or sedation.[16]

References 

 [1] Arnaldez F, Helman L (June 2012). "Targeting the insulin growth factor receptor 1". Hematol. Oncol. Clin. North Am. 26 (3): 527–42, vii–viii.doi: 10.1016/j.hoc.2012.01.004PMC 3334849PMID 22520978.

[2] McCarty M (1999). "Vegan proteins may reduce risk of cancer, obesity, and cardiovascular disease by promoting increased glucagon activity". Med. Hypotheses 53 (6): 459–85. doi:10.1054/mehy.1999.0784.PMID 10687887.

[3] Gallagher E, LeRoith D (April 2011). "Is growth hormone resistance/IGF-1 reduction good for you?". Cell Metab. 13 (4): 355–6.doi:10.1016/j.cmet.2011.03.003PMID 21459318.

[4]  Guevara-Aguirre, J; Balasubramanian, P; Guevara-Aguirre, M; Wei, M; Madia, F; Cheng, CW; Hwang, D; Martin-Montalvo, A et al. (2011). "Growth Hormone Receptor Deficiency Is Associated with a Major Reduction in Pro-Aging Signaling, Cancer, and Diabetes in Humans". Science Translational Medicine 3 (70): 70ra13.doi:10.1126/scitranslmed.3001845PMC 3357623.PMID 21325617.

[5] Bai, Nina. "Defective Growth Gene in Rare Dwarfism Disorder Stunts Cancer and Diabetes". Scientific American. Retrieved17 February 2011.

[6] Winerman, Lea. "Study: Dwarfism Gene May Offer Protection From Cancer, Diabetes"PBS. Retrieved 17 February 2011.

[7] Dermatology. 2012; 225(3):256-8. doi: 10.1159/000345102. Epub 2012 Dec 13. http://www.ncbi.nlm.nih.gov/pubmed/23257731

[8] Nestle Nutr Workshop Ser Pediatr Program. 2011; 67: 131-45. doi: 10.1159/000325580. E pub 2011 Feb 16. PMID: 21335995  http://www.ncbi.nlm.nih.gov/pubmed/21335995 

[9] Lactose Intolerance". Johns Hopkins Health Library. Retrieved 2014-02-18. 

[10] General guidelines for milk allergy". Oregon Health & Science University.

[11] Lactose Intolerance". National Digestive Diseases Information Clearinghouse (NDDIC). NIDDK. Retrieved 29 November 2011.

[12] Davidson, M, Kugler, MM, Baue, CH. Diagnosis and management in children with severe and protracted constipation and obstipation. J PEDIATR. 1963;62:261–275.

[13] Lothe, L, Lindberg, T. Cow's milk whey protein elicits symptoms of infantile colic in colicky formula-fed infants: a double- blind, crossover study. Pediatrics. 1989;83:262–266.

[14] Abrahamian, FP, Lloyd-Still, JD. Chronic constipation in childhood: a longitudinal study of 186 patients. J Pediatr Gastroenterol Nutr. 1984;3:460–467.

[15] J Nutr Biochem. 2014 Jan;25(1):36-43. doi: 10.1016/j.jnutbio.2013.08.012. Epub 2013 Oct 5.

[16] http://www.mayoclinic.org/drugs-supplements/whey-protein/safety/hrb-20060532
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The ‘What’, ‘Where’ and ‘Why’ of Carnitine

Carnitine is found in the bodies of all mammals and many other living organisms. Carnitine’s most well-known function is transporting fatty acids into each cell’s mitochondria (the energy center of the cell) for breakdown into energy.

The word carnitine is composed of the root word carne, meaning flesh. Red meat is a good source of carnitine but according to the National Institutes of Health (NIH), eating red meat can shorten your life span.[1]

Fortunately carnitine can be found in commonly consumed plants. There are a variety of sources including nuts and seeds. The following list has been compiled using radioisotopic technology to determine the carnitine content in common foods.[2] This list is by no means complete.

Listing higher sources first:

  • Tempeh 100 g contain 19.5 mg
  • Cod fish 100 g contain 5.6 mg
  • Chicken breast 100 g contain 3.9 mg
  • Whole milk 100 ml contain 3.3 mg
  • Potatoes 100 g contain 2.4 mg
  • Lentils 100 g contain 2.1 mg
  • Avocado one medium sized contains 2 mg
  • Sweet Potatoes 100 g contain 1.1 mg
  • Cottage cheese 100 g contain 1.1 mg
  • Raisins 100 g contain 0.8 mg
  • Whole wheat bread 100 g contain 0.36 mg
  • Carrots 100 g contain 0.3 mg
  • Bananas 100 g contain 0.2 mg
  • Apples (without skin) 100 g contain 0.2 mg
  • Asparagus 100 g contain 0.195 mg
  • White bread 100 g contain 0.147 mg
  • Peanut butter 100 g contain 0.083 mg
  • Rice 100 g contain 0.0449 mg
  • Egg 100 g contain 0.0121 mg
  • Orange juice 100 ml contain 0.0019 mg

When carnitine occurs in animal tissue, it is synthesized from the amino acids lysine and methionine. Humans synthesize carnitine in their bodies from these amino acids in the same manner that animals do.[3]

According to the National Institutes of Health, healthy children and adults do not need to consume carnitine from food or supplements because the liver and the kidneys produce sufficient amounts to meet daily needs.[4,5,6]

In 1989 The Food and Nutrition Board of the National Academies (formerly National Academy of Sciences) declared that carnitine was not an essential nutrient.[6]

Carnitine deficiencies are rare. Even strict vegetarians and vegans show no signs of carnitine deficiency.[7] The only time I have personally encountered a person deficient in carnitine was when they had been taking CoQ10 in doses of 200 mg a day for extended periods of time. This condition was easily corrected by taking a carnitine supplement and cutting back on CoQ10.

Studies that have been done using carnitine supplements to improve exercise performance show conflicting results. Some studies conclude no significant effect on exercise performance.[8][9] Other studies conclude a beneficial effect on training, competition and recovery from strenuous exercise.[10]

There are two main forms of carnitine supplements, L-carnitine and acetyl L-carnitine (also sometimes spelled acetylcarnitine or ALCAR).

The supplemental form called L-carnitine is usually taken by people trying to lose weight by converting their fat into energy. However, published studies showing the efficacy of using L-carnitine for weight loss are limited.

The form called acetyl L-carnitine is known to be more easily absorbed by the small intestine and is also known for its ability to pass through the blood brain barrier. Studies conclude that senior citizens with age related mental decline taking acetyl L-carnitine improved their mental functioning, especially in those with Alzheimer’s disease.[11][12]

In January of 2016 a meta-analysis of randomized controlled trials was published that showed a significant reduction of lipoprotein(a) levels following carnitine supplementation.[13] This is great news for those with genetically high Lp(a) levels because an elevated level of Lp(a) is a risk factor for heart disease and stroke.

One study found benefit for people with pancreatic cancer.[14]  Another study found benefit for people with diabetic peripheral neuropathy.[15]  Studies are ongoing about the use of carnitine supplements to treat various disease conditions.

Rare side effects of supplementing with carnitine include fishy body odor and rash. Taking large doses could result in nausea, diarrhea and cramps. People on prescription medication or those with heart disease, excessive, fatigue or a thyroid condition should talk to a doctor before taking carnitine.

For people who choose to supplement with carnitine I suggest using the product as directed on the label. No advantage appears to exist in taking an oral dose of carnitine greater than two grams at a time because absorption studies indicate saturation at this dose.[16]

By Craig B Sommers ND, CN

[1] http://www.nih.gov/news-events/nih-research-matters/risk-red-meat  

[2] Demarquoy, Jean; Georges, Béatrice; Rigault, Caroline; Royer, Marie-Charlotte; Clairet, Amélie; Soty, Maud; Lekounoungou, Serge; Le Borgne, Françoise (2004-06-01)."Radioisotopic determination of l-carnitine content in foods commonly eaten in Western countries". Food Chemistry 86 (1): 137–142. doi:10.1016/j.foodchem.2003.09.023

[3] http://www.ncbi.nlm.nih.gov/pubmed/21561431

[4] Rebouche CJ. Carnitine. In: Modern Nutrition in Health and Disease, 9th Edition (edited by Shils ME, Olson JA, Shike M, Ross, AC). Lippincott Williams and Wilkins, New York, 1999, pp. 505-12.

[5] The editors. Carnitine: lessons from one hundred years of research. Ann NY Acad Sci 2004;1033:ix-xi.

[6] National Research Council. Food and Nutrition Board. Recommended Dietary Allowances, 10th Edition. National Academy Press, Washington, DC, 1989.

[7] http://lpi.oregonstate.edu/infocenter/othernuts/carnitine/

[8] Brass EP. Supplemental carnitine and exercise. Am J Clin Nutr 2000;72:618S-23S.

[9] http://www.ncbi.nlm.nih.gov/pubmed/21561431

[10] http://www.ncbi.nlm.nih.gov/pubmed/15212755

[11] http://www.ncbi.nlm.nih.gov/pubmed/1944900

[12] http://www.ncbi.nlm.nih.gov/pubmed/18801359

[13] http://www.ncbi.nlm.nih.gov/pubmed/26754058

[14] http://www.ncbi.nlm.nih.gov/pubmed/22824168

[15] http://www.ncbi.nlm.nih.gov/pubmed/18940920

[16] Bain, Marcus A.; Milne, Robert W.; Evans, Allan M. (2006-10-01). "Disposition and metabolite kinetics of oral L-carnitine in humans". Journal of Clinical Pharmacology 46 (10): 1163–1170.doi:10.1177/0091270006292851. ISSN 0091-2700. PMID 16988205
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