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Egg white makes up around two-thirds of a chicken egg by weight. Water constitutes about 90% of this, with protein, trace minerals, fatty material, vitamins, and glucose contributing the remainder. [3] A raw U.S. large egg contains around 33 grams of egg white with 3.6 grams of protein, 0.24 grams of carbohydrate and 55 milligrams of sodium.
Asparagine, found abundantly in asparagus (hence, its name), is one of twenty of the most common amino acids and was the first amino acid to be isolated. While ovotransferrin identifies with its family, there are two types of ovotransferrin proteins: apo and holo. Apo-Ovotransferrin is deprived of iron and holo-Ovotransferrin is saturated with ...
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]
Ovomucin is a glycoprotein found mainly in egg whites, as well as in the chalaza and vitelline membrane. The protein makes up around 2-4% of the protein content of egg whites; like other members of the mucin protein family, ovomucin confers gel-like properties. It is composed of two subunits, alpha-ovomucin (MUC5B) and beta-ovomucin (MUC6), of ...
An ester of carboxylic acid. R stands for any group (organic or inorganic) and R′ stands for organyl group. In chemistry, an ester is a compound derived from an acid (organic or inorganic) in which the hydrogen atom (H) of at least one acidic hydroxyl group (−OH) of that acid is replaced by an organyl group (−R).
Phosvitin is one of the egg (commonly hen's egg) yolk [1] [2] phosphoproteins known for being the most phosphorylated protein found in nature. [3] [4] [5] Phosvitin isolation was first described by Mecham and Olcott in the year 1949. [3] [6] Recently [when?] it has been shown that phosvitin orchestrates nucleation and growth of biomimetic bone ...
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]
A 1991 assay for the Journal of Food Science detected substantial avidin activity in cooked egg white: "mean residual avidin activity in fried, poached and boiled (2 min) egg white was 33, 71 and 40% of the activity in raw egg white." The assay surmised that cooking times were not sufficient to adequately heat all cold spot areas within the egg ...