What is alpha lactalbumin allergy

Food allergies continue to be an significant human health problem. Recently, cases of food allergies own been increasing, with 5%–10% of infants and 1%–3% of school-age children in Japan affected by food allergies [1]. Hen eggs are most commonly responsible for food allergies, followed by cow milk. Patients with these food allergies develop adverse reactions, love urticaria, angioedema, wheezing, gastrointestinal symptoms, or anaphylactic shock, after ingestion of hen eggs, cow milk, or products that contain them.

Hen eggs are comprised of about 8%–11% shell, 56%–61% white, and 27%–32% yolk [2].

While the white is an aqueous protein solution (10% protein and 88% water), the yolk is composed of 50% water, 34% lipid, and 16% protein, giving it fairly diverse properties. Egg white has been considered the most significant source of allergens, with the ovomucoid (OMC; WHO/IUIS allergen name: Gal d 1), ovalbumin (Gal d 2), ovotransferrin (Gal d 3), and lysozyme C (Gal d 4) being the major allergens in it, but IgE-binding allergens own also been identified in the yolk. The characteristics of these four major egg white allergens are shown in Table 1. OMC and ovotransferrin are the most frequent allergens though it may depend on the reports.


Allergen name

Content in dried egg white (%)

Prevalence in patients (%)







Gal d 1



Gal d 2



Gal d 3



Gal d 4

Table 1. Major egg white allergens

pI: isoelectric point

Cow milk contains around 30–35 g of proteins per liter and includes more than 25 diverse proteins but only some of them are known to be allergenic.

Table 2 provides the characteristics of cow milk allergens. Cow milk proteins consist of the coagulum containing the casein proteins and the lactoserum (whey proteins) representing 80% and 20% of the entire milk proteins, respectively [3]. The casein part (Bos d 8) consists of four proteins that account for diverse percentages of the whole fraction: alphaS1-casein (Bos d 9), alphaS2-casein (Bos d 10), beta-casein (Bos d 11), and kappa-casein (Bos d 12), with alphaS1-casein being the most significant allergen of the casein part [4]. Allergens in the whey part are alpha-lactalbumin (Bos d 4), beta-lactoglobulin (BLG) (Bos d 5), immunoglobulins (Bos d 7), bovine serum albumin (BSA, Bos d 6), and traces of lactoferrin (Bos d lactoferrin).

Alpha-lactalbumin and beta-lactoglobulin are the most significant allergens of the whey part, accounting for 5% and 10% of the entire milk proteins, respectively [3,5]. There are only a few reports describing allergies to minor whey proteins such as immunoglobulin, BSA, or lactoferrin [6].


Allergen name



Prevalence in patients (%)

Size (kDa)






Bos d 4


Bos d 5

Bovine serum albumin

Bos d 6


Bos d 7






Bos d 9


Bos d 10


Bos d 11



Bos d 12


Table 2. Major cow milk allergens

pI: isoelectric point

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href=’/help/names_and_taxonomy_section’ target=’_top’>More</a></p>Names & Taxonomyi

<p>This subsection of the <a href=»»>Names and taxonomy</a> section provides an exhaustive list of every names of the protein, from commonly used to obsolete, to permit unambiguous identification of a protein.<p><a href=’/help/protein_names’ target=’_top’>More</a></p>Protein namesi

Recommended name:


Alternative name(s):

Lactose synthase B protein

Allergen: Bos d 4

<p>This subsection of the <a href=»»>Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry.

What is alpha lactalbumin allergy

Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href=’/help/gene_name’ target=’_top’>More</a></p>Gene namesi



<p>This subsection of the <a href=»»>Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href=’/help/organism-name’ target=’_top’>More</a></p>Organismi Bos taurus (Bovine)
<p>This subsection of the <a href=»»>Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein.

This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href=’/help/taxonomic_identifier’ target=’_top’>More</a></p>Taxonomic identifieri

<p>This subsection of the <a href=»»>Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href=’/help/taxonomic_lineage’ target=’_top’>More</a></p>Taxonomic lineagei cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos
<p>This subsection of the <a href=»»>Names and taxonomy</a> section is present for entries that are part of a <a href=»»>proteome</a>, i.e.

of a set of proteins thought to be expressed by organisms whose genomes own been completely sequenced.<p><a href=’/help/proteomes_manual’ target=’_top’>More</a></p>Proteomesi

  1. UP <p>A UniProt <a href=»»>proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href=’/help/proteome_component’ target=’_top’>More</a></p> Componenti: Unplaced

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href=’/help/function_section’ target=’_top’>More</a></p>Functioni

Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a excellent acceptor substrate for this enzyme.

What is alpha lactalbumin allergy

This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.

<p>The <a href=»»>Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary divide into 3 categories:<p><a href=’/help/gene_ontology’ target=’_top’>More</a></p>GO — Molecular functioni

Complete GO annotation on QuickGO


Feature key Position(s) DescriptionActions Graphical view Length
<p>This subsection of the <a href=»»>Function</a> section specifies the position(s) of the calcium-binding region(s) within the protein.

One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href=’/help/ca_bind’ target=’_top’>More</a></p>Calcium bindingi

97 – 

<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href=»/manual/evidences#ECO»>More</a></p> Manual assertion according to rulesi



GO — Biological processi

  1. lactose biosynthetic process
  2. defense response to Gram-negative bacterium <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href=»#iba»>GO evidence code guide</a></p> Inferred from biological aspect of ancestori
  3. response to deoxycorticosterone <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href=»#ida»>GO evidence code guide</a></p> Inferred from direct assayi
  4. response to dehydroepiandrosteroneInferred from direct assayi
  5. defense response to Gram-positive bacteriumInferred from biological aspect of ancestori
  6. response to estradiolInferred from direct assayi
  7. response to progesteroneInferred from direct assayi

Complete GO annotation on QuickGO

Enzyme and pathway databases

Reactome — a knowledgebase of biological pathways and processes


R-BTA Lactose synthesis


Hen egg allergy, cow milk allergy, ovomucoid, beta-lactoglobulin, electrolysis, S-S protein allergen

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href=’/help/subcellular_location_section’ target=’_top’>More</a></p>Subcellular locationi

  • Vilotte,J.L.; Soulier,S.; Mercier,J.C.; Gaye,P.; Hue-Delahaie,D.; Furet,J.P.

    Complete nucleotide sequence of bovine alpha-lactalbumin gene: comparison with its rat counterpart

    Biochimie 69 (), ()


  • Wang,M.; Scott,W.A.; Rao,K.R.; Udey,J.; Conner,G.E.; Brew,K.

    Recombinant bovine alpha-lactalbumin obtained by limited proteolysis of a fusion protein expressed at high levels in Escherichia coli


    Biol. Chem. (35), ()


  • Natale M; Bisson C; Monti G; Peltran A; Garoffo LP; Valentini S; Fabris C; Bertino E; Coscia A; Conti A


    Mol Nutr Food Res. Oct;48(5)


  • Jarvinen KM; Chatchatee P; Bardina L; Beyer K; Sampson HA

    IgE and IgG binding epitopes on alpha-lactalbumin and beta-lactoglobulin in cow

    Int Arch Allergy Immunol. Oct;(2)


  • Hurley WL; Schuler LA

    Molecular cloning and nucleotide sequence of a bovine alpha-lactalbumin cDNA.




  • Calvani M; Alessandri C; Frediani T; Lucarelli S; Miceli Sopo S; Panetta V; Zappalã D; Zicari AM

    Correlation between skin prick test using commercial extract of cow

    Pediatr Allergy Immunol.

    What is alpha lactalbumin allergy



  • Abstract

    Recently, public interest in food allergies has been increasing because of increasing prevalence of these allergies among children. In Japan, hen egg and cow milk allergies account for almost 50% of every cases of childhood food allergies. Patients with hen egg and cow milk allergies should avoid these foods and products that contain them until they own outgrown their allergies. However, regarding nutrition, quality of diet, and hyposensitization, it is significantly significant for these patients to ingest hypoallergenic hen eggs, cow milk, and products that contain them.

    We previously demonstrated the mitigation of the allergenic activity of beta-lactoglobulin in cow milk and ovomucoid in hen egg by electrolysis.

    What is alpha lactalbumin allergy

    In this review, we discuss this new strategy for producing hypoallergenic hen eggs and cow milk.

    Diagnosis of Hen Egg and Cow Milk Allergy and Effectiveness of The Skin Prick Test

    Conclusive diagnosis is crucial in patients with suspected food allergies. Double-blind, placebo-controlled food challenges are still the gold standard for diagnosing food allergies; however, these are time consuming, expensive, and troublesome for patients and involve risks of severe systemic reactions [7].

    Several diagnostic tests own been developed to predict outcomes of oral food challenges. Analysis of food-specific serum IgE levels [8,9], the skin prick test (SPT) [], and the atopy patch test [13] may be useful tools for diagnosing food allergies.

    However, the food challenge is still a crucial tool for definitively diagnosing food allergies, as analysis of food-specific serum IgE levels and the SPT do not currently render oral food challenges unnecessary in most cases [14]. The SPT is an significant first-line procedure for evaluating food allergies, as it is quick and relatively inexpensive. Previously, we reported that measuring wheal sizes in the SPT and calculating the skin index (SI) could assist diagnose numerous food allergies (e.g., to hen eggs, cow milk, wheat, and peanuts) [15]. Moreover, we performed the SPT in children suspected to own CMA and 76 had positive oral provocation test results.

    We performed a logistic regression analysis to assess whether wheal diameters or SIs could predict CMA in these patients.

    What is alpha lactalbumin allergy

    We found that wheal diameters and SIs could predict positive oral provocation test results. While the expected probabilities of having a positive oral provocation test result were ≥, the cut-off values for wheal diameters and SIs were ≥8 mm (% sensitivity and % specificity) and ≥ (% sensitivity and % specificity), respectively.

    Hill et al. [11] and Sporik et al. [16] showed that a 6-mm wheal diameter in children < 2 years of age, or 8 mm in children > 2 years of age, indicates % specificity of a clinical reaction.

    Saarinen et al. [17] reported 98% specificity and 92% positive predictive worth (PPV) for > 8-mm wheal diameter. Verstege et al.

    What is alpha lactalbumin allergy

    [12] reported 95% PPV for a mm wheal diameter when pricked with unused milk. Calvani et al.

    What is alpha lactalbumin allergy

    [18] reported 95% PPV for a mm wheal diameter in infants; this evidence supports results of our study, which shows that a mm wheal diameter had 90% PPV.