Vitamin B2, Whole Blood

CPT: 84252
Print Share


  • B2, Vitamin
  • Riboflavin
  • Vitamin B2, Quantitative

Expected Turnaround Time

3 - 5 days

Related Documents

Specimen Requirements


Whole blood, frozen and protected from light


0.5 mL

Minimum Volume

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


EDTA (lavender top) whole blood, preferred. Also acceptable are lithium heparin (green-top) whole blood and sodium heparin (light green-top) whole blood.


The blood is to be collected by venipuncture into a lavender-top tube containing EDTA and mixed immediately by gentle inversion at least six times to ensure adequate mixing. Do not separate. Transfer whole blood to a labeled amber plastic transport tube with amber stopper and freeze. For amber plastic transport tube and amber stopper, order Labcorp No. 23598.

If amber tubes are unavailable, cover standard transport tube completely, top and bottom, with aluminum foil. Identify specimen with patient's name directly on the container and the outside of the aluminum foil. Secure with tape.

To avoid delays in turnaround time when requesting multiple test on frozen samples, please submit separate frozen specimens for each test requested.

Storage Instructions

Specimens should be light-protected, stored frozen immediately, and maintained frozen during shipping.

Causes for Rejection

Receipt of non-frozen sample; receipt of plasma or serum specimen; receipt of specimen not protected from light

Test Details


Detect vitamin B2 deficiency


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

137−370 µg/L (Note: Reference interval reflects Flavin Adenine Dinucleotide (FAD), which accounts for approximately 90% of the total riboflavin in whole blood.)

Additional Information

Vitamin B2 refers to a family of water-soluble flavin vitamins that are critical for metabolism and energy generations in the aerobic cell, through oxidative phosphorylation.1-4 These compounds are synthesized in plants and microorganisms and occur naturally in three forms: the physiologically inactive riboflavin, and the physiologically active coenzymes flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD). FAD accounts for about 90% of the total riboflavin in tissues. Because of their capacity to transfer electrons, FAD and FMN are essential for proton transfer in the respiratory chain, for the dehydration of fatty acids, the oxidative deamination of amino acids, and for other redox processes.1-4 The effects of riboflavin deficiency on growth and development have generally been explained in terms of these functions. Flavin derivatives ingested with the diet (FAD, FMN) are dissociated by gastric acid from their protein binding, transformed by phosphatases to riboflavin, and absorbed in the small intestines.1,2 The reconversion of riboflavin to the coenzymes FMN and FAD occurs in the cytoplasm in many different tissues.

Vitamin B2 deficiency is common in many parts of the world, particularly in developing countries.1,5,6 Several studies have indicated that vitamin B2 deficiency may be widespread in industrialized countries as well, both in the elderly7,8 and in young adults.9 Dietary deficiency of riboflavin is characterized by lesions on the lips and the angles of the mouth, fissured and magenta-colored tongue, corneal vascularization and normocytic, normochromic anemia.1-4 Skin lesions include red scaly, greasy patches on the nose, eyelids, scrotum, and labia and seborrheic dermatitis.1-4 These symptoms are a consequence of oxidation stress due to the accumulation of lipid peroxides. Vitamin B2 deficiency leads to reduced activity of the flavin-containing enzymes (glutathione reductase and glutathione peroxidase) which, in turn, allows these peroxidase to express their deleterious effects.

Vitamin B2 is involved in the metabolism of folate, vitamin B12, vitamin B6, and other vitamins.10 Plasma vitamin B2 is a determinant of plasma homocysteine level, which is associated with cardiovascular disease, pregnancy complications, and cognitive impairment.10 Recent studies have suggested that riboflavin may play an important role in the determination of cell fate, which would have implications for growth and development.3 Specifically, riboflavin deficiency impairs the normal progression of the cell cycle, probably through effects on the expression of regulatory genes, exerted at both the transcriptional and proteomic level.3

No case of riboflavin toxicity in humans has been reported.


1. Ball GFM. Vitamins: their role in the human body. Oxford: Blackwell Publishing; 2004:289-299.
2. Rivlin RS, Pinto JT. Riboflavin (vitamin B2). In: Rucker RB, Suttie JW, McCormick DB, Machlin LJ, eds. Handbook of Vitamins. 3rd ed. New York, NY: Marcel Dekker; 2001:255-273.
3. Powers HJ. Riboflavin (vitamin B-2) and health. Am J Clin Nutr. 2003 Jun;77(6):1352-1360.12791609
4. Powers HJ, Corfe BM, Nakano E. Riboflavin in development and cell fate. Subcell Biochem. 2012;56:229-245.22116702
5. Bamji MS, Sarma KV, Radhaiah G. Relationship between biochemical and clinical indices of B-vitamin deficiency. A study in rural school boys. Br J Nutr. 1979 May;41(3):431-441.465434
6. Boisvert WA, Castañeda C, Mendoza I, et al. Prevalence of riboflavin deficiency among Guatemalan elderly people and its relationship to milk intake. Am J Clin Nutr. 1993 Jul;58(1):85-90.8317395
7. Bailey AL, Maisey S, Southon S, Wright AJ, Finglas PM, Fulcher RA. Relationships between micronutrient intake and biochemical indicators of nutrient adequacy in a ‘free-living’ elderly UK population. Br J Nutr. 1997 Feb;77(2):225-242.9135369
8. Madigan SM, Tracey F, McNulty H, et al. Riboflavin and vitamin B-6 intakes and status and biochemical response to riboflavin supplementation in free-living elderly people. Am J Clin Nutr. 1998 Aug;68(2):389-395.9701198
9. Benton D, Haller J, Fordy J. The vitamin status of young British adults. Int J Vitam Nutr Res. 1997;67(1):34-40.9119611
10. Hustad S, Ueland PM, Vollset SE, Zhang Y, Bjørke-Monsen AL, Schneede J. Riboflavin as a determinant of plasma total homocysteine: effect modification by the methylenetetrahydrofolate reductase C677T polymorphism. Clin Chem. 2000 Aug;46(8 Pt 1):1065-1071.10926884


Capo-chichi CD, Guéant JL, Lefebvre E, et al. Riboflavin and riboflavin-derived cofactors in adolescent girls with anorexia nervosa. Am J Clin Nutr. 1999 Apr;69(4):672-678.10197568
Hautem JY, Morel C, Couderc R, Moussa F. Liquid chromatographic determination of B(2) vitamers in human plasma and whole blood. Clin Chem. 2006 May;52(5):907-908.16638966
Hustad S, McKinley MC, McNulty H, et al. Riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in human plasma and erythrocytes at baseline and after low-dose riboflavin supplementation. Clin Chem. 2002 Sep;48(9):1571-1577.12194936
Midttun O, Hustad S, Solheim E, Schneede J, Ueland PM. Multianalyte quantification of vitamin B6 and B2 species in the nanomolar range in human plasma by liquid chromatography-tandem mass spectrometry. Clin Chem. 2005 Jul;51(7):1206-1216.15976101
Mulherin DM, Thurnham DI, Situnayake RD. Glutathione reductase activity, riboflavin status, and disease activity in rheumatoid arthritis. Ann Rheum Dis. 1996 Nov;55(11):837-840.8976642
Petteys BJ, Frank EL. Rapid determination of vitamin B₂ (riboflavin) in plasma by HPLC. Clin Chim Acta. 2011 Jan 14;412(1-2):38-43.20816949
Vasilaki AT, McMillan DC, Kinsella J, Duncan A, O’Reilly DS, Talwar D. Relation between riboflavin, flavin mononucleotide and flavin adenine dinucleotideconcentrations in plasma and red cells in patients with critical illness. Clin Chim Acta. 2010 Nov 11;411(21-22):1750-1755.20667447


Order Code Order Code Name Order Loinc Result Code Result Code Name UofM Result LOINC
123220 Vitamin B2, Whole Blood 6695-1 123221 Vitamin B2, Whole Blood ug/L 6695-1

For Providers

Please login to order a test

Order a Test

© 2021 Laboratory Corporation of America® Holdings and Lexi-Comp Inc. All Rights Reserved.

CPT Statement/Profile Statement

The LOINC® codes are copyright © 1994-2021, Regenstrief Institute, Inc. and the Logical Observation Identifiers Names and Codes (LOINC) Committee. Permission is granted in perpetuity, without payment of license fees or royalties, to use, copy, or distribute the LOINC® codes for any commercial or non-commercial purpose, subject to the terms under the license agreement found at Additional information regarding LOINC® codes can be found at, including the LOINC Manual, which can be downloaded at