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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]
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. It contains no cholesterol and the energy content is about 17 calories. [3] Egg white is an alkaline solution and contains around 149 proteins.
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 ]
However, albumin is lost at each process stage, with roughly 20% of the albumin lost through precipitation stages before fraction V. In order to purify the albumin, there is an extraction with water, and adjustment to 10% ethanol, pH of 4.5 at −3 °C. Any precipitate formed here is done so by filtration and is an impurity.
Ammonium sulfate is an inorganic salt with a high solubility that disassociates into ammonium (NH + 4) and sulfate (SO 2− 4) in aqueous solutions. [1] Ammonium sulfate is especially useful as a precipitant because it is highly soluble, stabilizes protein structure, has a relatively low density, is readily available, and is relatively inexpensive.
Albumin is a family of globular proteins, the most common of which are the serum albumins. All of the proteins of the albumin family are water-soluble, moderately soluble in concentrated salt solutions, and experience heat denaturation. Albumins are commonly found in blood plasma and differ from other blood proteins in that they are not ...
In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]
ion exchange on DEAE Sepharose is run to bind the albumin to the column, Albumin is eluted with a sodium acetate buffer, and; Final polishing with gel filtration. The end result is a highly pure and safe batch of albumin that is 100% non-pyrogenic, sterile, and free of active HIV virus. The product purity is greater than 98% and the protein ...