Delayed sensitivities to peptides in dairy can present up to 72 hours after consuming dairy foods. These sensitivities are based on IgG or IgA antibody-driven reactions and can affect both the local intestinal environment with acute symptoms, as well as the extra-intestinal systems from the skin, to the joints, brain, and other internal organs and tissue systems.
Detecting sensitivity to cow’s milk can be difficult due to its ubiquitous presence in the Western diet, symptom overlap with other common conditions, and the often delayed nature of sensitivity symptoms.
Vibrant has developed the Dairy Zoomer to answer the need for a comprehensive peptide-level test to detect with the highest sensitivity and specificity whether an individual is sensitive to any of the multiple peptides found in cow’s milk.
The Dairy Zoomer will also aid healthcare providers in determining if cow’s milk dairy may be at the root of an individual’s symptoms or medical conditions, and guide nutritional interventions based on specific lab results.
Only healthcare providers licensed in their state may order laboratory testing.
- αS1-casein & αS2-casein
- Beta-casomorphin (BCM 7)
- α -Lactalbumin
- ß – Lactoglobulin
- Serum albumin
If you have the following symptoms, you may be a good candidate for the Dairy Zoomer:
- Abdominal pain during or after meals
- Colic(in infants)
- Eczema or other rashes
- Mucous-filled cough
- Runny nose
- Eye irritation
- Recurring ear infections
- Other food sensitivities and allergies
- Atopic dermatitis
- Family history of dairy allergy
- Advanced age
Can the Vibrant Wellness Dairy Zoomer differentiate if a person can consume A1 vs. A2 milk?
Beta-casein (β-casein) is a 209 amino acid subunit of casein milk protein. The difference between the A1 and the A2 type β-casein variants is a single amino acid substitution at the 67th residue of the protein chain.
Thus, the ONLY difference in A1 and A2 variants is the amino acid at position 67.
A1 has histidine at position 67 whereas A2 has proline at position 67. Histidine does not bind as well as the amino acids positioned on either side of the chain and is more prone to cleavage during human digestion.
When A1 β-casein is metabolized, Beta casomorphin 7(BCM7/BCM), a peptide consisting of 7 amino acids with opioid properties, can break off; the immune system can potentially develop antibodies to this peptide independently.
Thus, if a person is ONLY producing antibodies to BCM7 (and does not react specifically to beta-casein) we can say this is a sensitivity specifically to A1 β-casein and not A2 β-casein.
If an individual shows an antibody response to β-casein only, we cannot differentiate if the sensitivity is to A1 vs. A2 casein. It is recommended to avoid all cow milk casein protein with this pattern of reactivity.
If someone is reactive (has elevated antibodies) on the Vibrant Wellness Dairy Zoomer, is it safe for them to consume other mammalian milks (e.g. goat milk, sheep milk,etc)?
The Vibrant Wellness Dairy Zoomer measures antibodies to peptides specific to cow milk only.
Different mammalian species will have different peptide/protein make up as they are genetically different species and proteins are derived from genes.
However, there is scientific uncertainty about cross-reactivity among mammalian milks. A provider needs to use clinical discretion and interpret a patient’s Dairy Zoomer results in context with history/symptoms and risk for reaction with other mammalian milks on an individualized basis.
Please note that Vibrant does offer protein-level food sensitivity testing specifically for GoatMilk (Food Sensitivity Profile I) and for Sheep Milk and Buffalo Milk (Food Sensitivity Profile II).
Dairy Sensitivity and Autoimmunity: What’s the Connection? https://vibrantwellnessblog.wordpress.com/2018/06/07/dairy-sensitivity-and-autoimmunity-whats-the-connection/
Are You Dairy Sensitive or Lactose Intolerant? What’s the Difference? https://vibrantwellnessblog.wordpress.com/2018/04/18/are-you-dairy-sensitive-or-lactose-intolerant-whats-the-difference/
- Davoodi SH, Shahbazi R, Esmaeili S, et al. Health-Related Aspects of Milk Proteins. Iranian Journal of
- Pharmaceutical Research: IJPR.2016;15(3):573-591.
- Pavia, Lampman, Kriz& Engel, Saunders. Isolation of Casein, Lactose, and Albumin from Milk Adapted by R. Minard (Penn State Univ.) from Introduction to Organic Laboratory Techniques: A Microscale Approach, 1990. Revised 3/20/2000
- Treweek T (2012). Alpha-Casein as a Molecular Chaperone, Milk Protein, In W. L. Hurley (Eds.), Milk Protein (pp. 85-119). Rijeka, Croatia: InTech
- Wildner G, Diedrichs-Möhring M. Autoimmune uveitis and antigenic mimicry of environmental antigens.
- Autoimmunity Reviews.2004;3:383-7
- Chin-Dusting J, Shennan J, Jones E, Williams C, Kingwell B and Dart A. Effect of dietary supplementation with beta-casein A1 or A2 on markers of disease development in individuals at high risk of cardiovascular disease. Br. J. Nutr.2006;95: 136-44.
- Karjalainen J1, Martin JM, Knip M, Ilonen J, Robinson BH, Savilahti E, Akerblom HK, Dosch HM. A bovine albumin peptide as a possible trigger of insulin-dependent diabetes mellitus. N Engl J Med. 1992;327(5):302-7.
- Laugesen M, Elliott R. Ischaemic heart disease, Type 1 diabetes, and cow milk A1 beta-casein. N Z Med J.
- 2003;116(1168): U295
- Elliott RB, Harris DP, Hill JP, Bibby NJ, Wasmuth HE. Type I (insulin-dependent) diabetes mellitus and cow
- milk: casein variant consumption. Diabetologia. 1999;42(3):292-6.
- Birgisdottir BE1, Hill JP, Thorsson AV, Thorsdottir I. Lower consumption of cow milk protein A1 beta-casein at 2 years of age, rather than consumption among 11- to 14-year-old adolescents, may explain the lower incidence of type 1 diabetes in Iceland than in Scandinavia. Ann NutrMetab. 2006;50(3):177-83
- Adler K, Mueller DB, Achenbach P, et al. Insulin autoantibodies with high affinity to the bovine milk protein alpha casein. Clinical and Experimental Immunology. 2011;164(1):42-49.
- Jianqin S, Leiming X, Lu X, Yelland GW, Ni J, Clarke A. Effects of milk containing only A2 beta casein versus milk containing both A1 and A2 beta casein proteins on gastrointestinal physiology, symptoms of discomfort, and cognitive behavior of people with self-reported intolerance to traditional cow’s milk. Nutrition Journal. 2016;15:35.
- Vacca-Smith A and Bowen W. The effect of milk and kappa casein on streptococcal glucosyltransferase.
- Caries Res. 1995; 29: 498-506
- Chia J S J, McRae J L, Kukuljan S et al. A1 beta-casein milk protein and other environmental pre-disposing
- factors for type 1 diabetes. Nutrition & Diabetes.2017;7: e274
- Niebuhr DW, Li Y, Cowan DN, Weber NS, Fisher JA, Ford GM, Yolken R. Association between bovine casein antibody and new onset schizophrenia among US military personnel. Schizophr Res. 2011 May;128(1-3):51-5.
- Severance EG, Dickerson FB, Halling M, Krivogorsky B, Haile L, Yang S, Stallings CR, Origoni AE, Bossis I, Xiao J, Dupont D, Haasnoot W, Yolken RH. Subunit and whole molecule specificity of the anti-bovine casein immune response in recent onset psychosis and schizophrenia. Schizophr Res. 2010 May;118(1-3):240-7 Davoodi, H., Esmaeili, S. and Mortazavian, A.M.. Effects of Milk and Milk Products Consumption on Cancer: A Review. Comprehensive Reviews in Food Science and Food Safety. 2013;12: 249-264.
- Luhovyy BL1, Akhavan T, Anderson GH. Whey proteins in the regulation of food intake and satiety. J Am Coll
- Brück W, Graverholt G and Gibson G. A two-stage continuous culture system to study the effect of supplemental α-lactalbumin and glycomacropeptide on mixed cultures of human gut bacteria challenged with enteropathogenic Escherichia coli and Salmonella serotype Typhimurium. J. Appl. Microbiol. 2003;95 : 44-53. Ng T, Lam T, Au T, Ye X and Wan C. Inhibition of human immunodeficiency virus type 1 reverse transcriptase, protease and integrase by bovine milk proteins. Life Sci.2001;69: 2217-23.
- De Wit J. Nutritional and functional characteristics of whey proteins in food products. J. Dairy Sci. 1998;81:
- Goldfarb M.F. Relation of Time of Introduction of Cow Milk Protein to an Infant and Risk of Type-1
- Mellitus. J, Proteome Res. 2008;7(5):2165-2167
- Ehn B M, Ekstrand B, Bengtsson U, Ahlstedt S. Modification of lgE Binding during Heat Processing of
- the Cow’s Milk Allergen a-Lactoglobulin. J. Agric. Food Chem. 2004; 52:1398-140
- the Cow’s Milk Allergen a-Lactoglobulin. J. Agric. Food Chem. 2004; 52:1398-140
- Diabetes Care. 1997;20(5):897-901.
- Huang BX, Kim HY, Dass C. Probing three-dimensional structure of bovine serum albumin
- by chemical
- cross-linking and mass spectrometry. J Am Soc Mass Spectrom.2004;15(8):1237-47.
- Farrell HM Jr, Jimenez-Flores R, Bleck GT, Brown EM, Butler JE, Creamer LK, Hicks CL,
- Hollar CM, Ng-Kwai-Hang KF, Swaisgood HE. Nomenclature of the proteins of cows’ milk–sixth
- revision. J Dairy Sci 2004;87(6):1641-74
- Giansanti F, Panella G, Leboffe L, Antonini G. Lactoferrin from Milk: Nutraceutical and
- Pharmacological Properties. Donno D, ed. Pharmaceuticals. 2016;9(4):61.
- Guggenmos J1, Schubart AS, Ogg S, Andersson M, Olsson T, Mather IH, Linington C. Antibody
- cross-reactivity between myelin oligodendrocyte glycoprotein and the milk protein
- butyrophilin in multiple sclerosis. J lmmunol. 2004;172(1):661-8.
- Stefferl A1, Schubart A, Storch2 M, Amini A, Mather I, Lassmann H, Linington C. Butyrophilin, a
- milk protein, modulates the encephalitogenic T cell response to myelin oligodendrocyte glycoprotein
- in experimental autoimmune encephalomyelitis. J lmmunol. 2000;165(5):2859-65.
- Vojdani, A et al. Antibodies to neuron-specific antigens in children with autism: possible
- cross-reaction with
- encephalitogenic proteins from milk, Chlamydia pneumoniae and Streptococcus group A
- Journal of
- Neuroimmunology. 2002;129(1):168 – 177