Ovalbumin

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Ovalbumin is the main protein found in egg white, making up 60-65% of the total protein (Huntington & Stein 2001). It belongs to the serpin superfamily of proteins, although unlike the majority of serpins it is unable to inhibit any proteases (Hunt & Dayhoff 1980). The function of ovalbumin is unknown, although it is presumed to be a storage protein (Gettins 2002). 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).

The ovalbumin protein of chickens is made up of 385 amino acids, and its relative molecular mass is 45 kD (Nisbet et al. 1981). It is a glycoprotein with 4 sites of glycosylation (Nisbet et al. 1981). It is secreted from the cell, despite lacking an N-terminal leader sequence (Robinson et al. 1986).

[edit] References

  • Gettins PGW (2002) Serpin structure, mechanism, and function. Chemical Reviews 102(12): 4751-4804.
  • 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.
  • Huntington JA, Stein PE (2001) Structure and properties of ovalbumin. Journal of Chromatography 756(1-2): 189-198.
  • 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.
  • Robinson A, Meredith C, Austen BM (1986) Isolation and properties of the signal region from ovalbumin. FEBS Letters 203(2): 243-246.
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