Ovalbumin is the main protein found in egg white, making up 60-65% of the total protein. Proteins are large Organic compounds made of Amino acids arranged in a linear chain and joined together by Peptide bonds between the Carboxyl Albumen redirects here For other uses see Albumen (disambiguation. [1] It belongs to the serpin superfamily of proteins, and like many serpins it is unable to inhibit any proteases. Serpins are a group of Proteins with similar structures that were first identified as a set of proteins able to inhibit Proteases The name serpin is derived A protease is any Enzyme that conducts Proteolysis, that is begins protein Catabolism by Hydrolysis of the Peptide bonds that link [2]
The function of ovalbumin is unknown, although it is presumed to be a storage protein. [3]
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). Proteomics is the large-scale study of Proteins particularly their structures and functions. Electrophoresis is the most well-known electrokinetic phenomenon.
- immunology (commonly used to stimulate an allergic reaction in test subjects). Immunology is a broad branch of biomedical Science that covers the study of all aspects of the Immune system in all Organisms It deals with Allergy is a disorder of the Immune system often also referred to as Atopy.
Structure
The ovalbumin protein of chickens is made up of 385 amino acids, and its relative molecular mass is 45 kDa. In Chemistry, an amino acid is a Molecule containing both Amine and Carboxyl Functional groups In Biochemistry, this The unified atomic mass unit ( u) or Dalton ( Da) or sometimes universal mass unit, is an unit of Mass used to express [4] It is a glycoprotein with 4 sites of glycosylation. Not to be confused with Peptidoglycan. Glycoproteins are proteins that contain Oligosaccharide chains ( Glycans) covalently attached [4]
It is secreted from the cell, despite lacking an N-terminal leader sequence. [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. Chelation is the binding or complexation of a bi- or multidentate Ligand.
References
- ^ 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.
External links
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