Sonia Ferveur/Sandbox
From Proteopedia
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[Ovalbumin]
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Ovalbumin (SERPINB14) is the main protein of the avian egg white. This protein represent approximatively 60% of the total protein. Its exact function is still unknown. Ovalbumin have sequence and three dimentional homology with the serpin superfamily. Serpin are serine protease inhibitor and can have also non inhibitory roles for exemple in hormone carriage proteins like Thyroxine-binding globulin and transcortin or molecular chaperoning (HSP47). Despite many similarities with serpin, Ovalbumin have no inhibitor properties but it is thought to be a storage protein for the developing foetus. In fact storage proteins are a reserve of ion and amino acid which can be used by organisms.
Properties
Ovalbumin can coagulated when heated: in solution at a concentration higher than 0.1% heated, a coagulum is formed.
Structure
Ovalbumin is a 42.8kDa protein consisting on 386 residus. It has a characteristic serpin domain consisting to 8-9 alpha helix and three beta sheets. Ovalbumin lacks a conformational change in the reactive center loop which confere the characteristic of a protease inhibitor to the serpin family. Ovalbumin tends to change into a more stable protein: S-ovalbumin.
Disease
Ovalbumin is one of the major allergens causing some children under 4 years old being highly sensitized to egg white. Ovalbumin sensitization is related to atopic dermatitis and children with ovalbumin sensitization are more likely to have asthma with atopic dermatitis, atopic dermatitis with allergic rhinitis, or atopic dermatitis, but are less likely to have asthma with allergic rhinitis. Atopic or allergic diseases causes a decrease of the titer of ovalbumin-IgG4 antibodies but an increase of ovalbumin-IgE antibodies.
Biotechnological use
Ovalbumin is used to induce asthma in rat, mouse and guinea pig to assess the in vivo efficacy of anti-asthma drugs.
Relevance
Structural highlights
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