Food:

BIOCHEMICAL INFORMATION for Egg (hen's egg)

Allergen Name:
Ovomucin
Alternatve Allergen Names:
None
Allergen Designation:
Minor
Protein Family:
There are multiple domains with 2 trypsin inhibitor like cysteine rich domains, a von Willebrand factor type C domain and 4 von Willebrand factor type D domains. Pfam PF01826; TIL; PF00093; VWC; PF00094; VWD. There are also other less annotated domains.
Sequence Known?:
Yes (alpha subunit). The beta subunit is a partial sequence.
Allergen accession No.s:

http://us.expasy.org/cgi-bin/niceprot.pl?Q98UI9 (alpha subunit)

http://us.expasy.org/cgi-bin/niceprot.pl?Q6L608 (beta subunit)
3D Structure Accession No.:
N/A
Calculated Masses:
233551 Da (alpha subunit precursor)
Experimental Masses:
Approximately 165 kDa (Awade et al. 1994 [1358])
Oligomeric Masses:

220 kDa - 270,000 kDa
Allergen epitopes:
Not known
Allergen stability:
Process, chemical, enzymatic
Not known
Nature of main cross-reacting proteins:
Not known
Allergen properties & biological function:
Ovomucin is heavily glycosylated and comprises approximately 3.5% of egg white protein. It has anti-viral activity.
Allergen purification:
Itoh et al. (1987) [1378], Rabouille et al (1990) [1379] and Awade et al (1994) [1358] report purifications of ovomucin. Awade et al. suggest that it is hard to produce a soluble pure preparation and that their own preparation is contaminated by ovostatin. However. other preparations may be contaminated by lysozyme.
Other biochemical information:

Alpha and beta subunits are homologous with 35% identity.

The reason that ovomucin has not been identified as an allergen in most studies of allergy to egg might be because many extraction procedures include a dialysis step and a centrifugation in order to get a "mucin free" solution to avoid mucin clogging chromatographic columns. However, the difficulty of purifying ovomucin free of other allergens may also be important.

References (5)

Awade AC, Moreau S, Molle D, Brule G, Maubois JL.
Two-step chromatographic procedure for the purification of hen egg white ovomucin, lysozyme, ovotransferrin and ovalbumin and characterization of purified proteins. J Chromatogr A 677(2):279-288. 1994
PUBMED ID: 7921188 		[1358]
Itoh, T.; Miyazaki, J.; Sugawara, H.; Adachi, S.
Studies on the characterization of ovomucin and chalaza of the hen's egg. J. Food Sci. 52, 1518-1521. 1987
PUBMED ID: unknown 		[1378]
Rabouille C, Aon MA, Muller G, Cartaud J, Thomas D.
The supramolecular organization of ovomucin. Biophysical and morphological studies. Biochem J. 266(3):697-706. 1990
PUBMED ID: 2327958 		[1379]
Walsh B, Hill Dj, Macoun P, Cairns D, Howden M.
Detection of four distinct groups of hen egg allergens binding IgE in the sera of children with egg allergy. Allergol Immunopathol (Madr). 33(4):183-191. 2005
PUBMED ID: 16045855 		[1646]
Walsh BJ, Barnett D, Burley RW, Elliott C, Hill DJ, Howden ME.
New allergens from hen's egg white and egg yolk. In vitro study of ovomucin, apovitellenin I and VI, and phosvitin. Int Arch Allergy Appl Immunol. 87(1):81-86. 1988
PUBMED ID: 3170012 		[1215]
This record was last modified on 18-Oct-2006
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