Biotin

244.31

244.31

200-399-3

6SO6U10H04

DTXSID7022679

C309

Long, thin needles from water|Colorless, crystalline

A - Alimentary tract and metabolism

29362930

104

0.3

White powder

1.42 g/cm³

232 °C (decomp)

573.6ºC at 760 mmHg

300.7ºC

90.5 ° (C=2, 0.1mol/L NaOH)

Soluble in hot water, dimethyl sulfoxide, alcohol and benzene.

Capsules and Tablets: Store below 40 deg C (104 deg F), preferably between 15 and 30 deg C (59 and 86 deg F), unless otherwise specified by manufacturer.

1.07X10-8 mm Hg at 25 deg C (est)

LD50 orally in Rabbit: > 2000 mg/kg

Henry's Law constant = 1.1X10-16 atm-cu m/mol at 25 °C (est)

150.4 Ų [M+H]+ [CCS Type: DT, Method: single field calibrated with Agilent tune mix (Agilent)]|152.96 Ų [M-H]- [CCS Type: DT, Method: single field calibrated with Agilent tune mix (Agilent)]|154.16 Ų [M+H]+ [CCS Type: DT, Method: stepped-field]|164.45 Ų [M+Na]+ [CCS Type: DT, Method: stepped-field]|159.72 Ų [M-H]- [CCS Type: DT, Method: stepped-field]|149.7 Ų [M+H]+ [CCS Type: DT, Method: single field calibrated with ESI Low Concentration Tuning Mix (Agilent)]|160.1 Ų [M+K]+ [CCS Type: DT, Method: single field calibrated with ESI Low Concentration Tuning Mix (Agilent)]|159.9 Ų [M+Na]+ [CCS Type: DT, Method: single field calibrated with ESI Low Concentration Tuning Mix (Agilent)]|155.4 Ų [M-H]- [CCS Type: DT, Method: single field calibrated with ESI Low Concentration Tuning Mix (Agilent)]|152.9 Ų [M+Na-2H]- [CCS Type: DT, Method: single field calibrated with ESI Low Concentration Tuning Mix (Agilent)]|148 Ų [M+H]+ [CCS Type: TW, Method: calibrated with polyalanine and drug standards]|152.9 Ų [M-2H+Na]-

Fine long needles. Melting point: 232-3 °C. pH 0.01% aq soln: 4.5. Isoelectric point pH: 3.5. Solubility in water, 2.20X10+2 mg/L at 25 °C. More sol in hot water and dil alkali; in 95% alc about 80 mg/100 ml at 25 °C; insol in other common org solvents. Specific optical rotation +91 deg at 21 °C (c=1, 0.1 N NaOH). The pure compd is stable to air and temp /Milk or liver biotin/|Water solutions are stable at 100 °C, and the dry substance is both thermostable and photostable. Biotin is unstable, however, in strong acids and alkaline solutions and in oxidizing agents.|Hydroxyl radical reaction rate constant = 4.0X10-11 cu cm/molec-sec at 25 °C (est)

1

R20/21/22; R36/37/38

24/25-36-26

XJ9088200

Xn

Stable, but light sensitive. Incompatible with strong oxidizing agents, strong bases, strong acids, formaldehyde, chloramine-T, nitrous acid.

SRP: The most favorable course of action is to use an alternative chemical product with less inherent propensity for occupational exposure or environmental contamination. Recycle any unused portion of the material for its approved use or return it to the manufacturer or supplier. Ultimate disposal of the chemical must consider: the material's impact on air quality; potential migration in soil or water; effects on animal, aquatic, and plant life; and conformance with environmental and public health regulations.

Incompatible with nitrous acid, oxidizing agents, formaldehyde, strong acid, or alkali.

Biotin used as a nutrient and/or dietary supplement in animal drugs, feeds, and related products is generally recognized as safe when used in accordance with good manufacturing or feeding practice.|Biotin used as a nutrient in food for human consumption is generally recognized as safe when used in accordance with good manufacturing practice.|Drug products containing certain active ingredients offered over-the-counter (OTC) for certain uses. A number of active ingredients have been present in OTC drug products for various uses, as described below. However, based on evidence currently available, there are inadequate data to establish general recognition of the safety and effectiveness of these ingredients for the specified uses: biotin is included in weight control drug products.|The Approved Drug Products with Therapeutic Equivalence Evaluations List identifies currently marketed prescription drug products, incl biotin, approved on the basis of safety and effectiveness by FDA under sections 505 of the Federal Food, Drug, and Cosmetic Act.

Not Classified

Prolonged skin contact may cause irritation.

Carbamazepine, phenytoin, and phenobarbital can accelerate biotin metabolism and may cause reduced biotin status. Long-term use of carbamazepine, phenytoin, phenobarbital and primidone has been associated with reduced plasma concentrations of biotin.|Antibiotic use may decrease the biotin contribution to the body made by the microflora of the large intestine.|Groups of Holtzman rats were mated and the gravid females were dosed sc with 100 mg D(+)-biotin in 0.2 mL of 0.1 N NaOH/kg body weight on days 0 and 1 of gestation. Nine animals were dosed with biotin only, 7 were given biotin and 0.1 ug 17(beta)-estradiol in 0.05 mL olive oil sc on days 5 to 20 of gestation, and 7 were given biotin and 4 mg progesterone in 0.2 mL olive oil sc on days 5 to 20 of gestation. Nine gravid animals were untreated and used as a negative-control group. Three groups of 6 nongravid animals were dosed in the same manner as the gravid animals and used as nonpregnant treated controls. The animals were killed and examined on day 21 of gestation. Complete resorption of the fetuses occurred in 8 of the 9 rats dosed with biotin only; dosing with estrogen or progesterone prevented the resorptions. Fetal and placental weights from animals dosed with biotin and estrogen or progesterone were decr as compared to controls, but the decr was not statistically significant. Biotin caused a decr in body weights of gravid and nongravid animals; body weights of gravid animals given biotin and progesterone were similar to gravid untreated control, whereas body weights of gravid animals given biotin and estrogen were incr. The uterine weights of gravid animals given biotin and estrogen were similar to that of gravid untreated controls, whereas the uterine weights of animals dosed with biotin and progesterone were statistically significantly decr.|...Groups of Holtzman rats were mated, and gravid females were dosed with 100 mg D(+)-biotin in 0.2 mL of 0.1 N NaOH/kg body weight on days 13 and 14 of gestation. Eleven animals were dosed with biotin only, 7 were given biotin and 0.1 ug 17(beta)-estradiol in 0.05 mL olive oil sc until day 20 of gestation, and 7 were given biotin and 4 mg progesterone in 0.2 mL olive oil sc until day 20 of gestation. Nine gravid animals were untreated and used as a negative-control group. The animals were killed and examined on day 21 of gestation. Resorptions occurred in 2 of the 11 animals dosed with biotin only. The maternal body weights and the fetal, uterine, and placental weights of the remaining 9 animals of this group were statistically significantly decr as compared to controls. The maternal body weights and the fetal, uterine, and placental weights of the animals dosed with biotin and estrogen and the maternal body weights and uterine weights of the animals dosed with biotin and progesterone were similar to control values. Hepatic and ovarian weights were similar for animals of the test and control groups.|For more Interactions (Complete) data for BIOTIN (6 total), please visit the HSDB record page.

LD50 Rat oral >1.45 mmol/kg|LD50 Mouse oral >10 g/kg

Growth factor present in very minute amt in every living cell. Plays in indispensable role in numerous naturally occurring carboxylation reactions. Occurs mainly bound to proteins or polypeptides. Richest sources are liver, kidney, pancreas, yeast, and milk. Biotin content of cancerous tumors is higher than that of normal tissue.|... biotin acts as a coenzyme for the body's carboxylation reaction and is a factor in maintaining healthy muscle, hair, nails, and skin.|BIOTIN IS PRESENT IN MOLASSES...NUTS, VEGETABLES & GRAINS. NATURALLY OCCURRING ISOMER IS D-BIOTIN; L-BIOTIN HAS NO BIOLOGICAL ACTIVITY.

The current recommendation for safe and adequate daily dietary intake of biotin for infants is based on measurements of biotin concentration in human milk and calculations of biotin intake that tacitly assume that biotin content of human milk is reasonably uniform for a given subject. This assumption of uniformity was tested by examining the effects of several factors on the biotin concentration. The degree of breast emptying had little effect on biotin concentration. However, in three of five individuals studied, the biotin concentration varied significantly over 24 hr. In two of five subjects, there was a consistent difference between breasts of approximately 16%. In the first 18 day postpartum, the milk concentration of biotin increased steadily in four of the eight individuals studied, remained low in two and increased erratically in two. Rather than reaching a stable plateau in mature milk, biotin concentration varied substantially in most of the subjects. These observations provide evidence that an adequate scheme for estimating total biotin intake of the breastfed infant will require sampling from both breasts frequently over the 24-hr cycle and frequently as a function of time postpartum.|Because estimates of the biotin requirement for infants currently are based on the biotin concentration in human milk, we sought to determine whether inactive biotin metabolites are present. Samples were collected for 7 weeks post partum from 15 healthy women. Biotin and the inactive metabolites bisnorbiotin and biotin sulfoxide were measured by means of a high-performance liquid chromatography avidin-binding assay. At 8 days post partum the proportion of biotin was 44%, bisnorbiotin 48%, and biotin sulfoxide 8%. Although biotin content increased post partum (p less than 0.003), the metabolites remained an important portion of the total providing evidence that accurate measurement of biotin in human milk requires an assay that is specific for biotin.

For nutritional supplementation, also for treating dietary shortage or imbalance.|Treatment of multiple sclerosis

Vitamin B refers to several water soluble vitamins often found together in foods, all of which are necessary for normal growth and metabolism, but none of which are synthesized in adequate amounts by humans. The common forms of vitamin B include vitamin B1 (thiamine), B2 (riboflavin), B3 (niacin), B6 (pyridoxine) and B12 (cyanocobalamin). Except for niacin (when given in high doses), there is no evidence that the other B vitamins, in physiologic or even super-physiologic high doses cause liver injury or jaundice. The major forms of vitamin B and selected other water soluble vitamins (biotin, pantothenic acid, choline) are discussed briefly in this record.

Vitamins

The B vitamins are indicated for prevention and treatment of vitamin B deficiency. Vitamin B deficiency may occur as a result of inadequate nutrition or intestinal malabsorption but does not occur in healthy individuals receiving an adequate balanced diet. Simple nutritional deficiency of individual B vitamins is rare since dietary inadequacy usually results in multiple deficiencies. For prophylaxis of biotin deficiency, dietary improvement, rather than supplementatin, is advisable. For teatment of biotin deficiency, supplementation is preferred. /Included in US product labeling/|Large doses of biotin ... are administered to babies with infantile seborrhea and to individuals with genetic alterations of biotin-dependent enzymes. patients who receive long-term parenteral nutrition should be given vitamin formulations that contain biotin.|(VET): Biotin is used as a feed additive for poultry and swine.|Biotin is used to treat the biotin-responsive inborn errors of metabolism holocarboxylase synthetase deficiency and biotinidase deficiency. Holocarboxylase deficiency is the most common cause of neonatal multiple carboxylase deficiency. Biotinidase deficiency is the most common cause of late-onset multiple carboxylase deficiency.|For more Therapeutic Uses (Complete) data for BIOTIN (11 total), please visit the HSDB record page.

Biotin deficiency, which can occur by the feeding of uncooked egg whites or by the omission of biotin from the diet, can cause alopecia and a characteristic scaly, erythematous dermatitis around body orifices in infants, children, and adults. For adults, prolonged biotin deficiency can result in depression, lethargy, hallucinations, and paresthesias of the extremities.|Biotin has not been proven effective in the treatment of acne, seborrheic eczema, or alopecia.

Biotin is a water-soluble B-complex vitamin which is composed of an ureido ring fused with a tetrahydrothiophene ring, which attaches a valeric acid substituent at one of its carbon atoms. Biotin is used in cell growth, the production of fatty acids, metabolism of fats, and amino acids. It plays a role in the Kreb cycle, which is the process in which energy is released from food. Biotin not only assists in various metabolic chemical conversions, but also helps with the transfer of carbon dioxide. Biotin is also helpful in maintaining a steady blood sugar level. Biotin is often recommended for strengthening hair and nails. Consequenty, it is found in many cosmetic and health products for the hair and skin. Biotin deficiency is a rare nutritional disorder caused by a deficiency of biotin. Initial symptoms of biotin deficiency include: Dry skin, Seborrheic dermatitis, Fungal infections, rashes including erythematous periorofacial macular rash, fine and brittle hair, and hair loss or total alopecia. If left untreated, neurological symptoms can develop, including mild depression, which may progress to profound lassitude and, eventually, to somnolence; changes in mental status, generalized muscular pains (myalgias), hyperesthesias and paresthesias. The treatment for biotin deficiency is to simply start taking some biotin supplements. A lack of biotin in infants will lead to a condition called seborrheic dermatitis or "cradle cap". Biotin deficiencies are extremely rare in adults but if it does occur, it will lead to anemia, depression, hair loss, high blood sugar levels, muscle pain, nausea, loss of appetite and inflamed mucous membranes.

A group of water-soluble vitamins, some of which are COENZYMES. (See all compounds classified as Vitamin B Complex.)

Systemic - approximately 50%|The intestine is exposed to biotin from a few sources: the diet, biotin supplements and biotin synthesized by bacteria in the large intestine. Dietary biotin exists in free and protein-bound forms. Protein-bound biotin is digested by proteases and peptidases to biotin-containing oligopeptides and biocytin (epsilon-N-biotinyl-L-lysine). Biocytin and the biotin-containing oligopeptides are converted to biotin via the enzyme biotinidase. Biotin - both dietary-derived biotin and supplementary biotin - is efficiently absorbed from the small intestine. At doses of biotin derived from food, biotin appears to be transported into enterocytes by a sodium -dependent carrier. At higher doses of biotin,absorption appears to occur by passive diffusion. Absorption of the biotin produced by the colonic microflora, appears to occur by a carrier mediated process in the proximal large intestine.|Elimination: Primarily in urine.|Protein binding: Primarily to plasma proteins.|Absorption: approximately 50%.|For more Absorption, Distribution and Excretion (Complete) data for BIOTIN (32 total), please visit the HSDB record page.

Biotin is excreted in the urine as biotin, bisnorbiotin, biotin sulfoxide, biotin sulfone, bisnorbiotin methyl ketone and tetranobiotin-1-sulfoxide.|Biotin is catabolized to a number of different metabolites, including bisnorbiotin, biotin sulfoxide, biotin sulfone, bisonorbiotin methylketone and tetranorbiotin-1-sulfoxide.|More than 95% of the biotin is free in the skim fraction of human milk. The concentration of biotin varies substantially in some women and exceeds that in serum by one to two order of magnitude, suggesting that there is a transport system into milk. The biotin metabolite bisnorbiotin accounts for approximately 50%. In early and transitional human milk, the biotin metabolite biotin sulfoxide accounts for about 10% of the total biotin plus metabolites. With postpartum maturation, the biotin concentration increases, but the bisnorbiotin and biotin sulfoxide concentrations still account for 25% and 8% at 5 weeks postpartum. Current studies provide no evidence for a soluble biotin-binding protein or any other mechanism that traps biotin in human milk.|On a molar basis, biotin accounts for approximately half of the total avidin-binding substances in human serum and urine. Biocytin, bisnorbiotin, bisnorbiotin methylketone, biotin sulfoxide, and biotin sulfone form most of the balance. Biotin metabolism is accelerated in some individuals by anticonvulsants and during pregnancy, thereby increasing the ratio of biotin metabolites to biotin excreted in urine.|An alternate fate to being incorporated into carboxylases or unchanged excretion is catabolism to an inactive metabolite before excretion in urine. About half of biotin undergoes metabolism before excretion. Two principal pathways of biotin catabolism have been identified in mammals. In the first pathway, the valeric acid side chain of biotin is degraded by beta oxidation. This leads to the formation of bisnorbiotin, tetranorbiotin, and related intermediates that are known to result from beta-oxidation of fatty acids. The cellular site of this beta-oxidation of biotin is uncertain. Nonenzymatic decarboxylation of the unstable beta-ketobiotin and beta-keto-bisnorbiotin leads to formation of bisnorbiotin methylketone and tetranorbiotin methylketone, which appear in urine. In the second pathway, the sulfur in the thiophane ring of biotin is oxidized, leading to the formation of biotin L-sulfoxide, biotin D-sulfoxide, and biotin sulfone. Combined oxidation of the ring sulfur and beta-oxidation of the side chain lead to metabolites such as bisnorbiotin sulfone. In mammals, degradation of the biotin ring to release carbon dioxide and urea is quantitatively minor.

Biotin is necessary for the proper functioning of enzymes that transport carboxyl units and fix carbon dioxide, and is required for various metabolic functions, including gluconeogenesis, lipogenesis, fatty acid biosynthesis, propionate metabolism, and catabolism of branched-chain amino acids.|In human tissues biotin is a cofactor for the enzymatic carboxylation of four substrates: pyruvate, acetyl coenzyme A (CoA), propionyl CoA, and beta-methylcrotonyl CoA. As such, it plays an important role in both carbohydrate and fat metabolism. Carbon dioxide fixation occurs in a two-step reaction, the first involving binding of carbon dioxide to the biotin moiety of the holoenzyme, and the second involving transfer of the biotin-bound carbon dioxide to an appropriate acceptor.|Biotin functions in carbon dioxide fixation reactions in intermediate metabolism, transferring the carboxyl group to acceptor molecules. It acts similarly in decarboxylation reactions. Biotin is essential in human metabolism for its part in the previously described enzymatic steps, in catalyzing deamination of amino acids, and in oleic acid synthesis. Biotin is a cofactor for the enzymatic carboxylation of pyruvate, acetyl coenzyme A (CoA), propionyl CoA, and beta-methylcrotonyl CoA, and, therefore, plays an important role in carbohydrate and fat metabolism.|Protein folding in the endoplasmic reticulum (ER) depends on Ca2+; uptake of Ca2+ into the ER is mediated by sarco/endoplasmic reticulum Ca2+-ATPase 3 (SERCA3). The 5'-flanking region of the SERCA3 gene (ATP2A3) contains numerous binding sites for the transcription factors Sp1 and Sp3. Biotin affects the nuclear abundance of Sp1 and Sp3, which may act as transcriptional activators or repressors. Here we determined whether biotin affects the expression of the SERCA3 gene and, thus, protein folding in human lymphoid cells. Jurkat cells were cultured in media containing 0.025 nmol/L biotin (denoted "deficient") or 10 nmol/L biotin ("supplemented"). The transcriptional activity of the full-length human SERCA3 promoter was 50% lower in biotin-supplemented cells compared to biotin-deficient cells. Biotin-dependent repressors bind to elements located 731 to 1312 bp upstream from the transcription start site in the SERCA3 gene. The following suggest that low expression of SERCA3 in biotin-supplemented cells impaired folding of secretory proteins in the ER, triggering unfolded protein response: (i) sequestration of Ca2+ in the ER decreased by 14 to 24% in response to biotin supplementation; (ii) secretion of interleukin-2 into the extracellular space decreased by 75% in response to biotin supplementation; (iii) the nuclear abundance of stress-induced transcription factors increased in response to biotin supplementation; and (iv) the abundance of stress-related proteins such ubiquitin activating enzyme 1, growth arrest and DNA damage 153 gene, X-box binding protein 1 and phosphorylated eukaryotic translation initiation factor 2alpha increased in response to biotin supplementation. Collectively, this study suggests that supplements containing pharmacological doses of biotin may cause cell stress by impairing protein folding in the ER.|Evidence is emerging that biotin participates in processes other than classical carboxylation reactions. Specifically, novel roles for biotin in cell signaling, gene expression, and chromatin structure have been identified in recent years. Human cells accumulate biotin by using both the sodium-dependent multivitamin transporter and monocarboxylate transporter 1. These transporters and other biotin-binding proteins partition biotin to compartments involved in biotin signaling: cytoplasm, mitochondria, and nuclei. The activity of cell signals such as biotinyl-AMP, Sp1 and Sp3, nuclear factor (NF)-kappaB, and receptor tyrosine kinases depends on biotin supply. Consistent with a role for biotin and its catabolites in modulating these cell signals, greater than 2000 biotin-dependent genes have been identified in various human tissues. Many biotin-dependent gene products play roles in signal transduction and localize to the cell nucleus, consistent with a role for biotin in cell signaling. Posttranscriptional events related to ribosomal activity and protein folding may further contribute to effects of biotin on gene expression. Finally, research has shown that biotinidase and holocarboxylase synthetase mediate covalent binding of biotin to histones (DNA-binding proteins), affecting chromatin structure; at least seven biotinylation sites have been identified in human histones. Biotinylation of histones appears to play a role in cell proliferation, gene silencing, and the cellular response to DNA repair. Roles for biotin in cell signaling and chromatin structure are consistent with the notion that biotin has a unique significance in cell biology.

Biotin, which is to be not less than 97.5% and more than 100.5% by assay, may contain < 3 ppm arsenic and < 10 ppm heavy metals (as Pb) ...|One company requires that biotin contain <0.25% diamino derivative, biotinylbiotin, and monobenzyl biotin ... /Another company/ reports that biotin contains <10 mg/kg heavy metals (as Pb).

/SRP:/ Basic treatment: Establish a patent airway (oropharyngeal or nasopharyngeal airway, if needed). Suction if necessary. Watch for signs of respiratory insufficiency and assist ventilations if needed. Administer oxygen by nonrebreather mask at 10 to 15 L/min. Monitor for pulmonary edema and treat if necessary ... . Monitor for shock and treat if necessary ... . Anticipate seizures and treat if necessary ... . For eye contamination, flush eyes immediately with water. Irrigate each eye continuously with 0.9% saline (NS) during transport ... . Do not use emetics. For ingestion, rinse mouth and administer 5 ml/kg up to 200 ml of water for dilution if the patient can swallow, has a strong gag reflex, and does not drool ... . Cover skin burns with dry sterile dressings after decontamination ... . /Poisons A and B/|/SRP:/ Advanced treatment: Consider orotracheal or nasotracheal intubation for airway control in the patient who is unconscious, has severe pulmonary edema, or is in severe respiratory distress. Positive-pressure ventilation techniques with a bag valve mask device may be beneficial. Consider drug therapy for pulmonary edema ... . Consider administering a beta agonist such as albuterol for severe bronchospasm ... . Monitor cardiac rhythm and treat arrhythmias as necessary ... . Start IV administration of D5W /SRP: "To keep open", minimal flow rate/. Use 0.9% saline (NS) or lactated Ringer's if signs of hypovolemia are present. For hypotension with signs of hypovolemia, administer fluid cautiously. Watch for signs of fluid overload ... . Treat seizures with diazepam or lorazepam ... . Use proparacaine hydrochloride to assist eye irrigation ... . /Poisons A and B/

/OTHER TOXICITY INFORMATION/ Biotin toxicity has not been reported in man despite administration of large amounts for as long as 6 months.|/OTHER TOXICITY INFORMATION/ Biotin-responsive basal ganglia disease (BBGD) is a recessive disorder with childhood onset that presents as a subacute encephalopathy, with confusion, dysarthria, and dysphagia, and that progresses to severe cogwheel rigidity, dystonia, quadriparesis, and eventual death, if left untreated. BBGD symptoms disappear within a few days with the administration of high doses of biotin (5 to 10 mg/kg/day). On brain magnetic resonance imaging examination, patients display central bilateral necrosis in the head of the caudate, with complete or partial involvement of the putamen. All patients diagnosed to date are of Saudi, Syrian, or Yemeni ancestry, and all have consanguineous parents. Using linkage analysis in four families ... /the authors/ mapped the genetic defect near marker D2S2158 in 2q36.3 (LOD=5.9; theta=0.0) to a minimum candidate region (approximately 2 Mb) between D2S2354 and D2S1256, on the basis of complete homozygosity. In this segment, each family displayed one of two different missense mutations that altered the coding sequence of SLC19A3, the gene for a transporter related to the reduced-folate (encoded by SLC19A1) and thiamin (encoded by SLC19A2) transporters.

Biodermatin

BIOTIN IS COMMERCIALLY AVAILABLE AS THE CRYSTALLINE D-ISOMER...NOT WIDELY USED IN FOOD FORTIFICATION.|The amount of the vitamin in a product is expressed solely in terms of the weight of the chemically pure substance, the free monocarboxylic acid.|Oral: Capsules: 1000 ug (1 mg) (OTC) (GENERIC).|Oral: Tablets: 300 ug (0.3 mg), 400 ug (0.4 mg) 600 ug (0.6 mg) and 800 ug (0.8 mg) (OTC) (GENERIC).|Number of formulations containing biotin (FDA 1998): bubble baths 1/200; other eye makeup preparations /than mascara/ 2/120; hair conditioners 20/636; shampoos--noncoloring 11/860; tonics, dressings, and other hair-grooming aids 7/549; other hair preparations 2/276; foundations 2/287; bath soaps and detergents 2/385; cleansing preparations 1/653; face and neck preparations--excluding shaving 1/263; body and hand preparations--excluding shaving 1/796; moisturizing preparations 5/769; night preparations 4/188; paste masks/mud packs 2/255; skin fresheners 2/184; other skin care preparations 6/692; indoor tanning preparations 1/62; other suntan preparations 1/38. Current /biotin/ concn of use (CTFA 1999): mascara 0.0001%; other eye makeup preparations 0.01%; hair conditioners 0.0001% to 0.01%; shampoos--noncoloring 0.0001% to 0.001%; tonics, dressings, and other hair-grooming aids 0.001%; foundations 0.0001% to 0.001%; face and neck preparations--excluding shaving 0.002% to 0.6%; moisturizing preparations 0.005%.

1H-Thieno[3,4-d]imidazole-4-pentanoic acid, hexahydro-2-oxo-, (3aS,4S,6aR)-: ACTIVE|ISOLATION FROM EGG YOLK: KOGL, TONNIS, Z PHYSIOL CHEM 242, 43 (1936); FROM LIVER: GYORGY ET AL, J BIOL CHEM 131, 745 (1939); DU VIGNEAUD ET AL, IBID 140, 643 (1941). IDENTITY OF BIOTIN WITH VIT H: DU VIGNEAUD ET AL, SCIENCE 92, 62 (1940).|THERE IS NO OFFICIAL PREPN OF BIOTIN, & SINGLE-ENTITY PREPN OF THE CMPD ARE NOT MARKETED IN US.|THREE FORMS OF BIOTIN...HAVE BEEN DERIVED FROM NATURAL MATERIAL. THESE DERIVATIVES ARE BIOCYTIN (EPSILON-N-BIOTINYL-L-LYSINE) & D & L SULFOXIDES OF BIOTIN. DERIVED FORMS...ARE ACTIVE IN SUPPORTING GROWTH OF SOME MICROORGANISMS.|US RECOMMENDED DAILY ALLOWANCE PERMITS INCLUSION OF 0.15 MG BIOTIN IN MULTIVITAMIN SUPPLEMENTS FOR INFANTS & CHILDREN & 0.3 MG IN SUPPLEMENTS FOR ADULTS.|For more General Manufacturing Information (Complete) data for BIOTIN (10 total), please visit the HSDB record page.

AFTER SIMPLE AQ OR ACID EXTRACTION COMBINED WITH HEATING, MICROBIOLOGICAL ASSAY USING GROWTH OF TEST ORGANISMS ALLESHERIA BOYDII OR LACTOBACILLUS ARABINOSUS AS CRITERION IS CARRIED OUT.|TLC DETERMINATION OF BIOTIN IN A LYOPHILIZED MULTIVITAMIN PREPN.|Analyte: biotin; matrix: chemical identification; procedure: infrared absorption spectrophotometry with comparison to standards|Analyte: biotin; matrix: chemical purity; procedure: dissolution in water; addition of phenolphthalein indicator; titration with sodium hydroxide|For more Analytic Laboratory Methods (Complete) data for BIOTIN (20 total), please visit the HSDB record page.

A microbiological, an avidin-binding and a streptavidin-binding method for biotin determination were compared. All three methods detected biotin equally well but they exhibit different specificities for derivatives of biotin. The microbiological assay has the highest specificity and is the method of choice for biotin determination in biotinidase-deficient patients. The specificity of streptavidin-binding has not been investigated so far. Application of the three methods to urine samples of patients with and without biotin therapy indicated that only 50% of biotin equivalents measured with the avidin method correspond to authentic biotin as previously shown. The other 50% comprise mainly bisnorbiotin and biotin-d-sulfoxide. HPLC-separation of urine samples prior to assay confirmed this finding and revealed a bisnorbiotin oxidation product and an unknown compound as further biotin metabolites. The latter was measurable by all three methods and not detectable in plasma ultrafiltrate. This was the only metabolite which was able to restore deficient 3-methylcrotonyl-CoA carboxylase activity in biotin-deficient fibroblasts. The combination of the three methods together with HPLC-separation proved to be a valuable analytical tool for the identification of the main biotin metabolites in biological fluids.|The biotin content of plant and animal food samples as well as of human plasma and urine specimens was assessed by a modified protein binding assay (PBA). Protein bound biotin in samples was released by digestion with papain, food samples were in addition treated previously with liquid nitrogen. Comparing analyses by use of the conventional microbiological test with Lactobacillus plantarum resulted in slightly enhanced biotin values, in case of plasma by 9.2% and in case of urine by 10.3%, but the results obtained by both methods correlated well (r = 0.926 for plasma and 0.934 for urine). Regarding food analysis the additional comparison of different disintegration procedures led to best reproducible results by using the PBA with preceding papain digestion.|An improved agar plate method of biotin bioassay using Lactobacillus plantarum ATCC 8014 and bromocresol purple was established to determine biotin levels in human serum and urine. Samples were treated with 4.5 N H2SO4 to liberate free biotin, autoclaved for 1 hr and neutralized by 4.5 N NaOH, then 10 microliters was added to wells in each plate. The biotin levels were measured in 190 serum and 59 urine samples, and the means were 2.7 + or - 0.53 ng/mL and 12.4 + or - 5.56 ng/mg of creatinine, respectively. The intra-assay coefficient varience (CV) were 3.2 (n = 20) and 1.3% (n = 23), respectively. The recovery of biotin added (10 ng/mL) to serum was 110.7%, and to urine was 99.6%. These findings suggest that this assay is sufficiently accurate and reproducible for routine use in the clinical laboratory. The excretion of orally administered biotin was also demonstrated by the method.

Human Drugs -> EU pediatric investigation plans|Human Drugs -> FDA Approved Drug Products with Therapeutic Equivalence Evaluations (Orange Book) -> Active Ingredients|Cosmetics -> Antiseborrhoeic; Hair conditioning; Skin conditioning