View source for Ovalbumin

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==Overview==
Ovalbumin is the main [[protein]] found in egg white, making up 60-65% of the total protein.<ref>Huntington JA, Stein PE (2001) Structure and properties of ovalbumin. Journal of Chromatography B 756(1-2): 189-198.</ref> It belongs to the [[serpin]] superfamily of proteins, although unlike the majority of serpins it is unable to inhibit any [[protease]]s.<ref>Hunt LT, Dayhoff MO (1980) A surprising new protein superfamily containing ovalbumin, antithrombin-III, and alpha 1-proteinase inhibitor. Biochemical and biophysical research communications 95(2): 864-871.</ref> 

The function of ovalbumin is unknown, although it is presumed to be a storage protein.<ref>Gettins PGW (2002) Serpin structure, mechanism, and function. Chemical Reviews 102(12): 4751-4804.</ref>

==Research==
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 [[allergy|allergic reaction]] in test subjects).

==Structure==
The ovalbumin protein of chickens is made up of 385 [[amino acid]]s, and its relative molecular mass is 45 kD.<ref name="Nisbet">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.</ref> It is a [[glycoprotein]] with 4 sites of glycosylation.<ref name="Nisbet"> </ref>

It is secreted from the cell, despite lacking an N-terminal leader sequence.<ref>Robinson A, Meredith C, Austen BM (1986) Isolation and properties of the signal region from ovalbumin. FEBS Letters 203(2): 243-246.</ref>
 
==Medicinal characteristics==
In cases where poisoning by heavy metals (such as Iron) is suspected, ovalbumin may be administered.<ref>Dominiczak M, Baynes J Medical Biochemistry, 2d edition, p59.</ref> Ovalbumin chelates to heavy metals and traps the metal ions within the sulfhydryl bonds of the protein. Chelating prevents the absorption of the metals into the gastrointestinal tract and prevents poisoning.

==References==
<references/>

==External links==
* {{MeshName|Ovalbumin}}

{{Serpins}}
{{Albumins}}


[[Category:Proteins]]
[[Category:Hematology]]

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