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Ovalbumin (abbreviated OVA [1]) is the main protein found in egg white, making up approximately 55% of the total protein. [2] Ovalbumin displays sequence and three-dimensional homology to the serpin superfamily, but unlike most serpins it is not a serine protease inhibitor. [ 3 ]
The 3D structure of human serum albumin has been determined by X-ray crystallography to a resolution of 2.5 ångströms (250 pm). [1] Albumin is a 65–70 kDa protein. Albumin comprises three homologous domains that assemble to form a heart-shaped protein. [2] Each domain is a product of two subdomains that possess common structural motifs. [2]
Ovalbumin is the most abundant protein in albumen. Classed as phosphoglycoprotein, during storage, it converts into s-ovalbumin (5% at the time of laying) and can reach up to 80% after six months of cold storage. Ovalbumin in solution is heat-resistant. Denaturation temperature is around 84 °C, but it can be easily denatured by physical stresses.
Some storage proteins store amino acids. Storage proteins' amino acids are used in embryonic development of animals or plants. Two amino acid storage proteins in animals are casein and ovalbumin. Seeds, particularly of leguminous plants, contain high concentrations of storage proteins. Up to 25 percent of the dry weight of the seed can be ...
The general structure of albumin is characterized by several long α helices allowing it to maintain a relatively static shape, which is essential for regulating blood pressure. Serum albumin contains eleven distinct binding domains for hydrophobic compounds. One hemin and six long-chain fatty acids can bind to serum albumin at the same time. [7]
Ovalbumin is the protein which makes up around two-thirds of the white of an egg. [14] When an egg is cooked, the ovalbumin changes conformation from its folded and soluble form to an insoluble all-β-sheet structure with exposed hydrophobic regions, leading to aggregation. [15]
Ovotransferrin makes up approximately 13% of egg albumen (in contrast to ovalbumin, which comprises 54%). [2] As a member of the transferrin and metalloproteinase family, ovotransferrin has been found to possess antibacterial and antioxidant and immunomodulatory properties, arising primarily through its iron (Fe3+) binding capacity by locking ...
11657 Ensembl ENSG00000163631 ENSMUSG00000029368 UniProt P02768 P07724 RefSeq (mRNA) NM_000477 NM_009654 RefSeq (protein) NP_000468 NP_033784 Location (UCSC) Chr 4: 73.4 – 73.42 Mb Chr 5: 90.61 – 90.62 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Human serum albumin is the serum albumin found in human blood. It is the most abundant protein in human blood plasma ; it ...