Sources
Help build the largest human-edited directory on the web.
Submit a site - Become an editor
Wikipedia. Licensed under the GNU Free Documentation License.
Are you an expert in this subject? Join the discussion and share your knowledge at Wikipedia.org.
Ovalbumin
From Wikipedia, the free encyclopedia
Ovalbumin is the main protein found in egg white, making up 60-65% of the total protein.[1] It belongs to the serpin superfamily of proteins, although unlike the majority of serpins it is unable to inhibit any proteases.[2]
The function of ovalbumin is unknown, although it is presumed to be a storage protein.[3]
Contents |
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.[4] It is a glycoprotein with 4 sites of glycosylation.[4]
It is secreted from the cell, despite lacking an N-terminal leader sequence.[5]
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.
- ^ Huntington JA, Stein PE (2001) Structure and properties of ovalbumin. Journal of Chromatography B 756(1-2): 189-198.
- ^ 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.
- ^ 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.
Alpha 1-antichymotrypsin - Alpha 1-antitrypsin - Alpha 2-antiplasmin - Antithrombin - C1-inhibitor - Heat shock protein 47 - Heparin cofactor II - Protein C inhibitor - Plasminogen activator inhibitor-1 - Plasminogen activator inhibitor-2 - Protein Z-related protease inhibitor
noninhibitory: Maspin - Ovalbumin - Thyroxine-binding globulin - Transcortin