Ovalbumin is the main protein found in egg white, making up 60-65% of the total protein.[1] While Ovalbumin displays sequence and three-dimensional homology to the serpin superfamily, it is a noninhibitory serpin [2]. While most serpins control such processes as fibrinolysis and coagulation by inhibiting serine proteases, the function of ovalbumin is unknown, although it is presumed to be a storage protein.[3]
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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 allergic reaction in test subjects, e.g. established model allergen for airway hyper-responsiveness AHR).
(For in-vivo and in-vitro studies based on ovalbumin it is important that the endotoxin content is less than 1 EU/mg.)[citation needed]
Structure
The ovalbumin protein of chickens is made up of 385 amino acids, and its relative molecular mass is 45 kDa.[4] It is a glycoprotein with 4 sites of glycosylation.[4]
It is secreted from the cell. Unlike the signal sequences of most secreted proteins, Ovalbumin's signal sequence is not cleaved. Additionally it is not located directly on the N-terminus, but rather internally, starting at residue 21 and ending at residue 47. [5]
Medicinal characteristics
In cases where poisoning by heavy metals (such as Iron) is suspected, ovalbumin may be administered.[6] 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
- ^ Huntington JA, Stein PE (2001) Structure and properties of ovalbumin. Journal of Chromatography B 756(1-2): 189-198.
- ^ Hu H.Y., Du H.N. (2000). "Alpha to Beta Structural Transformation of Ovalbumin: Heat and pH Effects.". Journal of Protein Chemistry 19 (3): 177–183. doi:.
- ^ Gettins PGW (2002) Serpin structure, mechanism, and function. Chemical Reviews 102(12): 4751-4804.
- ^ a b 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.
- ^ Dominiczak M, Baynes J Medical Biochemistry, 2d edition, p59.
See also
External links
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