Ovalbumin

File:Ovalbumin.png

Ovalbumin structure

Ovalbumin is the main protein found in egg white, making up approximately 55% of the total protein content. It is a member of the serpin superfamily, although it does not have protease inhibitory activity like many other serpins. Ovalbumin is used extensively in research as a model protein due to its abundance and ease of purification.

Structure

Ovalbumin is a glycoprotein with a molecular weight of approximately 45 kDa. It consists of a single polypeptide chain of 385 amino acids. The protein has a complex tertiary structure stabilized by disulfide bonds and hydrogen bonding. The three-dimensional structure of ovalbumin has been determined by X-ray crystallography, revealing a compact, globular shape.

Function

Although ovalbumin is a member of the serpin family, it does not function as a protease inhibitor. Its biological role is not entirely clear, but it is thought to serve as a storage protein in egg white, providing a source of amino acids for the developing embryo. Ovalbumin also plays a role in the viscosity and foaming properties of egg white, which are important for culinary applications.

Applications in Research

Ovalbumin is widely used in biochemical and immunological research. It serves as a model antigen in studies of immune responses, particularly in the context of allergy and asthma research. Ovalbumin is often used to induce experimental allergic reactions in animal models, allowing researchers to study the mechanisms of hypersensitivity and inflammation.

Related pages

• Egg white
• Protein structure
• Serpin
• Glycoprotein