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The ovalbumin protein of chickens consists of 385 amino acids, its relative molecular mass is 42.7 kDa, [5] and it adopts a serpin-like structure. [6] Ovalbumin also has several modifications, including N-terminal acetylation (G1), phosphorylation (S68, S344), and glycosylation (N292). [5]
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.
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 composed of storage proteins. The best known storage protein in wheat is the prolamin gliadin, a component of gluten.
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]
Egg white albumen is composed of multiple proteins, of which ovotransferrin is the most heat reliable. It has a molecular weight of 76,000 daltons and contains about 700 amino acids. Ovotransferrin makes up approximately 13% of egg albumen (in contrast to ovalbumin, which comprises 54%). [2]
Leukocyte elastase inhibitor (LEI) also known as serpin B1 is a protein that in humans is encoded by the SERPINB1 gene. It is a member of the clade B serpins or ov-serpins (ovalbumin related serpins) founded by ovalbumin. [5] [6] [7] MNEI (monocyte/neutrophil elastase inhibitor) is the mouse orthologue of human SerpinB1. [7]
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]