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Warnings

Do not give riboflavin to a child without medical advice.

Ask a doctor or pharmacist if it is safe for you to use riboflavin if you have other medical conditions, especially:

• gallbladder disease; or
• cirrhosis or other liver disease.

Riboflavin is considered likely safe to use during pregnancy, but your dose needs may be different during this time. You should not use riboflavin without a doctor's advice if you are pregnant.

Interactions

There are no known significant interactions.

Food interaction

Pregnancy

• Your name may need to be listed on an antiviral pregnancy registry when you start using this medication.
• Avloclor and Paludrine should not be used during pregnancy unless, in the judgement of the physician, potential benefit outweighs the risk.
• Can I still use over the counter natural cream to help support pregnancy.

Overview

Riboflavin (vitamin B2 preparation). We studied the effect of the additional consumption of riboflavin on the physical performance of 14 Canadian highly qualified swimmers with the normal status for this vitamin and its dietary intake consistent with the recommended standards. The subjects of one subgroup took it at a dose of 60 mg per day for 16–20 days, whereas for the subjects of the other subgroup, the drug was replaced with a placebo. Physical performance was assessed in the swimming test, which using this in sixfold overcoming the 50-meter distance freestyle. In addition, the maximum aerobic power and ventilation anaerobic threshold were determined in the treadmill test. The drug significantly increases visual acuity and resistance to hypoxia; however, the consumption of riboflavin in lengthy tests did not affect either its level in the blood or physical performance. It was concluded that during sports training, swimmers can fully maintain their normal riboflavin status without additional consumption of this vitamin. In addition, it is obviously necessary to work out its dosages for athletes specializing in shooting, as well as in other sports, taking into account the antihypoxic effect.

Vitamin B2 by itself does not have anabolic activity, and its coenzyme forms - riboflavin mononucleotide and flavinate, which are not produced in Ukraine, possess. Drugs activate enzymes involved in the synthesis of amino acids, lipids and carbohydrates. They normalize the course of redox processes, cholesterol metabolism, enhance hemoglobin synthesis, accelerate iron absorption, and improve vision. For a growing organism, these drugs are an indispensable growth factor.

Pharmacological group: vitamins; water soluble vitamins; B vitamins
IUPAC name: 7,8-Dimethyl-10 - [(2S, 3S, 4R) -2,3,4,5-tetrahydroxypentyl] benzo [g] pteridin-2, 4-dione
Molecular Formula C₁₇H_twentyN_fourO₆
Molar mass 376.36 g mol-1
Appearance: orange crystals
Acidity (pKa) 9.888
Basicity (PCB) 4.109

Riboflavin, also known as Vitamin B2, is an easily absorbable colored trace element that plays a key role in maintaining human and animal health. It is a central component of the cofactors FAD (flavin adenine dinucleotide) and FMN (flavin mononucleotide), and therefore is necessary for all flavoproteins. Thus, vitamin B2 is important for a variety of cellular processes. It plays a key role in energy metabolism, as well as in the metabolism of fats, ketone bodies, carbohydrates and proteins. Milk, cheese, leafy vegetables, liver, kidneys, legumes, yeast, mushrooms and almonds are good sources of vitamin B2, but exposure to light destroys riboflavin. The name "riboflavin" comes from the words "ribose" (sugar, the restored form of which, ribite, is part of its structure) and "flavin", the ring part that gives the oxidized molecule a yellow color (from Latin flavus, "yellow"). The reduced form, which occurs in metabolism along with the oxidized form, is colorless. Riboflavin is visually known as a vitamin that gives orange color to solid B-vitamin preparations, yellow to solutions of vitamin supplements, and an unusual fluorescent yellow color to the urine of people taking high-dose vitamin B drugs. Riboflavin can be used as an orange-red colored food supplement and, as such, has the E number E101 in Europe.

Opening

Initially, it was believed that vitamin B consists of two components, thermolabile vitamin B1 and heat-resistant vitamin B2. In the 1920s, vitamin B2 was considered a substance necessary for the prevention of pellagra. In 1923, Paul Gyorgy from Heidelberg examined biotin deficiency in rats; Vitamin H (now called Biotin or Vitamin B7) was considered the curative factor of this disease. Since pellagra and vitamin H deficiency were associated with dermatitis, Gyorgy decided to test the effect of vitamin B2 on vitamin H deficiency in rats. He enlisted the support of Wagner-Djurreg from Kuhn's laboratory. In 1933, Kuhn, György, and Wagner discovered that thiamine-free extracts of yeast, liver, or rice bran interrupted growth in rats fed with foods containing thiamine supplements. In addition, the researchers noted that the yellow-green fluorescence in each extract contributed to the growth of rats, and that the fluorescence intensity was proportional to the effect on growth. This observation made it possible to develop a method of rapid B2-Max and biological analysis to isolate a substance from egg protein in 1933, which they called ovoflavin. The same group then isolated the same drug (growth promoting compound with yellow-green fluorescence) from serum using the same procedures (lactoflavin). In 1934, the Kuhn group was able to determine the structure of the so-called flavin and synthesize vitamin B2.

Biochemical functions

Flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) function as coenzymes for a wide range of oxidative enzymes and remain bound to the enzymes during redox reactions. Flavins can act as oxidizing agents due to their ability to take a pair of hydrogen atoms. The contraction of the isoalloxazine ring (FAD, FMN oxidized form) leads to the creation of a reduced form of flavoproteins (FMNH2 and FADH2).

The mechanism of action as cofactors and flavoproteins

Flavoproteins exhibit a wide range of redox potential and, therefore, can play a variety of roles in intermediate metabolism. Some of these roles are: • flavoproteins play an important role in the electron transfer chain • FAD is required in the decarboxylation of pyruvate and α-KG • in fatty acyl-CoA dehydrogenase FAD is required for the oxidation of fatty acids • FAD is required for the production of pyridoxic acid from pyridoxal (vitamin B6) • The main form of coenzyme of vitamin B6 (pyridoxal phosphate) depends on FMN • FAD is required to convert retinol (vitamin A) to retinoic acid • synthesis of the active form of folic acid (5-methyl THF) depends on FADH2 • FAD is required for To convert tryptophan to niacin (Vitamin B3) • Reduction of the oxidized form of glutathione (GSSG) to the reduced form (GSH) also depends on FAD

Riboflavin in Foods: Origin, Sources, and Stability

Riboflavin is a yellow or yellow-orange substance that is used not only as a food coloring, but also to enrich certain foods, such as baby food, breakfast cereals, pastas, sauces, processed cheese, fruit drinks, fortified dairy products and some energy drinks. Yeast extract is considered the main source of vitamin B2, and the liver and kidneys are also rich in them. In addition, vitamin B2 is also found in wheat bran, eggs, meat, milk and cheese. Flavins are found in relatively low concentrations in cereals, but they are the main source of flavins in countries where cereals form the basis of the diet. Grinding cereals leads to significant (up to 60%) loss of vitamin B2, therefore, in some countries, for example, in the USA, enrichment of white flour is practiced. The fortification of bread and ready-to-eat breakfast cereal significantly increases the value of the diet and its vitamin B2 content. Polished rice is usually not enriched, since the yellow color, which gives it vitamin B2, reduces its attractiveness in the eyes of buyers. However, most of the flavin contained in whole brown rice is preserved if the rice is steamed before chopping. During this process, the flavins located in the embryo and the aleuron layer pass into the endosperm. Free riboflavin is naturally present in foods, along with binding to FMN and FAD proteins. Cow's milk contains mostly free riboflavin, and small amounts of FMN and FAD. In whole milk, 14% of flavins non-covalently binds to specific proteins. Egg white and yolk contain special riboflavin-binding proteins, which are necessary to maintain free riboflavin in the egg for use by a developing embryo. It is rather difficult to include riboflavin in most liquid products, since it has poor solubility in water, and therefore, riboflavin-5'-phosphate (E101a), a more expensive but more soluble form of riboflavin, is used instead. Riboflavin, when cooked and cooked without exposure to light, is generally stable. An alkaline environment in which riboflavin may be unstable is rarely found in food. Riboflavin degradation in milk may occur more slowly in the dark when stored in the refrigerator.

Recommended Diet

The latest (1998) vitamin B2 recommendations are similar to the 1989 recommendations, where the minimum intake for adults was 1.2 mg for people whose total food intake is more than 2000 kcal per day. Currently, riboflavin intake rates for adult men and women are 1.3 mg / day and 1.1 mg / day, respectively. The expected average intake for adult used for and women is 1.1 mg and 0.9 mg, respectively. During pregnancy and lactation, it is recommended to increase the daily intake of riboflavin to 1.4 mg and 1.6 mg, respectively. For infants, consumption rates are 0.3-0.4 mg / day, and for children 0.6-0.9 mg / day.

Riboflavin deficiency

In healthy people, riboflavin is constantly excreted in the urine, so a deficiency with insufficient intake is quite common. However, a deficiency of riboflavin is always accompanied by a deficiency of other vitamins. Riboflavin deficiency can be primary (with a lack of vitamins in the daily diet), or secondary, which may be the result of conditions that affect intestinal absorption when the body is unable to use the consumed vitamin, or with increased excretion of the vitamin from the body. In humans, signs and symptoms of riboflavin deficiency (ariboflavinosis) include cracks and redness on the lips, inflammation of the mucous membrane of the mouth and tongue, mouth ulcers, cracks in the corners of the mouth (angular cheilitis) and sore throat. Deficiency can also cause dryness and peeling of the skin, the formation of fluid in the mucous membranes, and iron deficiency anemia. Redness of the eyes, itching, tearing, and increased sensitivity to bright light may also be show. Riboflavin deficiency is classically associated with oral-genital-ocular syndromes. Angular cheilitis, photophobia, and scrotum dermatitis are classic symptoms of deficiency. In animals, riboflavin deficiency leads to stunting, weight loss, and ultimately death. The experimental results of riboflavin deficiency in dogs caused stunting, weight loss, ataxia, and inability to stand up. Animals weakened, fell into a coma and died. With deficiency, dermatitis develops along with hair loss. Other signs include corneal opacity, cataracts, Waterhouse-Friedericksen syndrome (acute adrenal insufficiency), fatty degeneration of the kidneys and liver, and inflammation of the gastrointestinal mucosa. Post-mortem studies of rhesus monkeys on a riboflavin-deficient diet revealed that only about one open page of the normal amount of riboflavin was present in their liver (the main organ for storing riboflavin in mammals). Such clear clinical signs of riboflavin deficiency are rare among residents of developed countries. However, about 28 million Americans have a common “subclinical” deficit, characterized by a change in biochemical parameters (for example, a decrease in plasma levels of red blood cell glutathione reductase). Although the effects of long-term subclinical riboflavin deficiency are unknown, in children this deficiency leads to reduced growth. Subclinical riboflavin deficiency is also observed in women taking oral contraceptives, in the elderly, in people with eating disorders and in painful conditions such as HIV, inflammatory bowel disease, diabetes mellitus and chronic heart disease. The fact that riboflavin deficiency does not immediately lead to gross clinical manifestations indicates that systemic levels of this essential vitamin are tightly regulated.

Riboflavin Status Assessment

To confirm clinical cases with riboflavin deficiency and to establish subclinical deficiencies, biochemical tests are necessary. These tests include:

• Activity of erythrocyte glutathione reductase:
Glutathione reductase is nicotinamide adenine dinucleotide phosphate (NADPH), FAD (flavin adenine dinucleotide) is a dependent enzyme, and it is also the main flavoprotein in red blood cells. Measurement of the erythrocyte activity coefficient of glutathione reductase (EHR) is the preferred method for assessing the status of riboflavin. This provides a measure of tissue saturation and the long-term status of riboflavin. Under laboratory conditions, enzyme activity in B2-Max of activity coefficient (CA) is also determined without adding FAD to the medium. CA is the ratio of enzyme activity to FAD, according to the activity of the enzyme without FAD. With CA from 1.2 to 1.4, the status of riboflavin is considered low, with the addition of FAD to stimulate enzymatic activity. With CA> 1.4, riboflavin deficiency begins. On the other hand, with the addition of FAD and CA Vitamin, water-soluble vitamins, B vitamins, energy, metabolism, fat metabolism, ketone metabolism, carbohydrate metabolism, protein metabolism, cooking, nutritional supplements, ariboflavinosis, lip cracks, lip redness, mucosal inflammation membranes B2-Max the mouth, inflammation of the mucous membrane of the tongue, ulcers of the oral cavity, angular cheilitis, sore throat, dry skin, peeling of the skin, iron deficiency anemia, redness of the eyes, itching, lacrimation, oral-genital-ocular syndromes, photophobia, d scrotum rmatitis, vitamin deficiency, growth retardation, weight loss, ataxia, dermatitis (eczema), hair loss (baldness), corneal opacity, cataracts, Waterhouse-Friedericksen syndrome, fatty degeneration of the kidneys, fatty degeneration of the liver, inflammation of the mucous membrane of the gastrointestinal tract, migraine, keratoconus, Brown – Vialetto – van Laer syndrome, Fazio-Londe syndrome, industrial products

Vitamin B2 has a lot of names - riboflavin, lactoflavin, lactoben, ribovin. Almost all of these names indicate a method for producing vitamin, and most of all, riboflavin in milk, eggs, liver and some types of plants (for example, in legumes).

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