Vitamin B7

CPT: 84591
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  • Biotin

Expected Turnaround Time

2 - 7 days

Related Documents

Specimen Requirements


Serum or plasma


1 mL

Minimum Volume

0.5 mL (Note: This volume does not allow for repeat testing.)


Red-top tube or lavender-top (EDTA) tube


Transfer separated serum or plasma to a plastic transport tube. Include the patient's age on the test request form.

Storage Instructions


Stability Requirements



Room temperature

3 days


3 days


14 days

Freeze/thaw cycles

Stable x3

Causes for Rejection

Gel-barrier tube

Test Details


Measurement of vitamin B7 level


This test was developed and its performance characteristics determined by LabCorp. It has not been cleared or approved by the Food and Drug Administration.


Liquid chromatography/tandem mass spectrometry (LC/MS-MS)

Reference Interval

0.05−0.83 ng/mL

Additional Information

Biotin is a colorless, water-soluble B-complex vitamin that is also referred to as vitamin B7.1-3 Biotin functions as a cofactor for five mammalian enzymes that catalyze specific carboxylation reactions.2 These are:

• Acetyl-CoA carboxylase I and II: catalyze the carboxylation of acetyl CoA to form malonyl CoA which, in turn, serves as a substrate for fatty acid elongation. These enzymes function in cytosolic fatty acid synthesis and in regulating mitochondrial fatty acid oxidation.

• Pyruvate carboxylase: catalyzes the carboxylation of pyruvate to form oxaloacetate, which serves as an intermediate in the citric acid cycle. This reaction is involved in gluconeogenesis, the production of glucose from other carbohydrates by the liver, kidney, and other gluconeogenic tissues.

• Methylcrotonyl-CoA carboxylase: catalyzes an essential step in the catabolism of leucine, an essential, branch-chained amino acid.

• Propionyl-CoA carboxylase: catalyzes essential steps in the metabolism of several amino acids, cholesterol, and odd chain fatty acids.1

Biotin is also covalently attached to histone proteins that are essential for the folding of DNA into chromatin. It has been suggested that the biotinylation of histones might play a role in cell proliferation, gene silencing, and cellular response to DNA damage.4

Clinically advanced biotin deficiency is rare in the general population; however, significant biotin deficiency can occur in individuals who consume raw egg white over long periods.1,2 Avidin, an antimicrobial protein found in egg white, binds biotin and prevents its absorption. Cooking egg white denatures avidin and wipes out its biotin-binding capacity.1 Profound biotin deficiency can also occur in cases of drastically diminished biotin absorption (patients taking total parenteral nutrition without biotin and in some malabsorption conditions).1,2 Some forms of liver disease may increase the requirement for biotin and result in clinical deficiency.1,5 Patients receiving long-term anticonvulsant medication may also be at increased the risk for biotin deficiency.1,2 The results of several studies suggest that biotin deficiency may also be relatively common during pregnancy.1,6

Physical findings associated with overt biotin deficiency include a red scaly rash around the eyes, nose, mouth, and genital area.1-3,7 Some reports suggest that biotin deficiency may result in brittle finger nails and that high dose supplementation may, to some extent, ameliorate the condition.1,2,7 Adults with this deficiency experience thinning of hair, frequently with loss of hair color. Reported neurologic symptoms have included depression, lethargy, hallucination, and paresthesia of the extremities. Individuals with hereditary disorders of biotin metabolism also suffer from impaired immune system function and susceptibility to bacterial and fungal infections.1-3,8


1. Oregon State University, Linus Pauling Institute Micronutrient Research Center. Niacin. Available at: Accessed January 7, 2011.
2. Food and Nutrition Board, Institute of Medicine, Pantothenic Acid. Dietary Reference Intakes: Thiamin, Riboflavin, Niacin, Vitamin B6, Vitamin B12, Pantothenic Acid, Biotin, and Choline. Washington, DC: National Academy Press;1998:357-373.
3. Mock DM. Biotin. In: Ziegler EE, Filer LJ Jr, eds. Present Knowledge in Nutrition. 7th ed. Washington, DC: ILSI Nutrition Foundation;1996: 220-235.
4. Kothapalli N, Camporeale G, Kueh A, et al. Biological functions of biotinylated histones. J Nutr Biochem. 2005 Jul; 16(7):446-448. 15992689
5. Pabuçcuoğlu A, Aydoğdu S, Baş M. Serum biotinidase activity in children with chronic liver disease and its clinical significance. J Pediatr Gastroenterol Nutr. 2002 Jan; 34(1):59-62. 11753166
6. Mock DM. Marginal biotin deficiency is common in normal human pregnancy and is highly teratogenic in mice. J Nutr. 2009 Jan; 139(1):154-157. 19056637
7. Biotin. Altern Med Rev. 2007 Mar; 12(1)73-78. 17397270
8. Mardach R, Zempleni J, Wolf B, et al. Biotin dependency due to a defect in biotin transport. J Clin Invest. 2002 Jun; 109(12):1617-1623. 12070309


Order Code Order Code Name Order Loinc Result Code Result Code Name UofM Result LOINC
070097 Vitamin B7 1980-2 070098 Vitamin B7 ng/mL 1980-2

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