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ovalbumin, ovalbumin allergy
Ovalbumin abbreviated OVA[1] is the main protein found in egg white, making up approximately 55% of the total protein[2] Ovalbumin displays sequence and three-dimensional homology to the serpin superfamily, but unlike most serpins it is not a serine protease inhibitor[3] The function of ovalbumin is unknown, although it is presumed to be a storage protein[4]


  • 1 Research
  • 2 Structure
    • 21 Change upon heating
  • 3 See also
  • 4 References
  • 5 External links


Ovalbumin is an important protein in several different areas of research, including:

  • general studies of protein structure and properties because it is available in large quantities
  • studies of serpin structure and function the fact that ovalbumin does not inhibit proteases means that by comparing its structure with that of inhibitory serpins, the structural characteristics required for inhibition can be determined
  • proteomics chicken egg ovalbumin is commonly used as a molecular weight marker for calibrating electrophoresis gels
  • immunology commonly used to stimulate an allergic reaction in test subjects, eg established model allergen for airway hyper-responsiveness, AHR

For in vivo and in vitro studies based on ovalbumin it is important that the endotoxin content is less than 1 EU/mg[citation needed]


The ovalbumin protein of chickens consists of 385 amino acids, its relative molecular mass is 427 kDa,[5] and it adopts a serpin-like structure[6] Ovalbumin also has several modifications, including N-terminal acetylation G1, phosphorylation S68, S344, and glycosylation N292[5] It is secreted from the cell, targeted by an internal signal sequence residues 21-47, rather than the N-terminal signal sequence commonly found in other secreted proteins Ovalbumin's signal sequence is not cleaved off, but remains as part of the mature protein[7]

Change upon heating

When heated, ovalbumin undergoes a conformational change from its soluble, serpin structure into an insoluble all-β-sheet structure with exposed hydrophobic regions This causes the protein to aggregate and cause the solidification associated with cooked egg white[8]

See also

  • Egg allergy


  1. ^ Sano Kunio; Kanna Haneda; Gen Tamura; Kunio Shirato 1999 "Ovalbumin OVA and Mycobacterium tuberculosis Bacilli Cooperatively Polarize Anti-OVA T-helper Th Cells toward a Th1-Dominant Phenotype and Ameliorate Murine Tracheal Eosinophilia" Am J Respir Cell Mol Biol 20 6: 1260–1267 doi:101165/ajrcmb2063546 Retrieved 28 December 2011 
  2. ^ Takehiko Yamamoto, Mujo Kim, Hen eggs 
  3. ^ Hu HY, Du HN 2000 "Alpha to Beta Structural Transformation of Ovalbumin: Heat and pH Effects" Journal of Protein Chemistry 19 3: 177–183 doi:101023/A:1007099502179 PMID 10981809 
  4. ^ Gettins, PGW 2002 "Serpin structure, mechanism, and function" Chemical Reviews 102 12: 4751–4804 doi:101021/cr010170+ 
  5. ^ a b Nisbet, AD; Saundry, RH; Moir, AJG; Fothergill, LA; Fothergill, JE 1981 "The complete amino-acid sequence of hen ovalbumin" European Journal of Biochemistry 115 2: 335 doi:101111/j1432-10331981tb05243x 
  6. ^ Stein, Penelope E; Leslie, Andrew G W; Finch, John T; Carrell, Robin W 1991-10-05 "Crystal structure of uncleaved ovalbumin at 1·95 Å resolution" Journal of Molecular Biology 221 3: 941–959 doi:101016/0022-28369180185-W 
  7. ^ Robinson, A; Meredith, C; Austen, BM 1986 "Isolation and properties of the signal region from ovalbumin" FEBS Letters 203 2: 243–246 doi:101016/0014-57938680751-7 
  8. ^ Hu, H Y; Du, H N 2000-04-01 "α-to-β Structural Transformation of Ovalbumin: Heat and pH Effects" Journal of Protein Chemistry 19 3: 177–183 doi:101023/A:1007099502179 ISSN 0277-8033 PMID 10981809 

External links

  • Ovalbumin at the US National Library of Medicine Medical Subject Headings MeSH

ovalbumin, ovalbumin allergy, ovalbumin amino acid sequence, ovalbumin and ovomucoid, ovalbumin chemical formula, ovalbumin function, ovalbumin in vaccines, ovalbumin protein, ovalbumin sigma, ovalbumin structure

Ovalbumin Information about


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    Ovalbumin beatiful post thanks!


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