About 50 percent of the proteins of egg white are composed of ovalbumin, which is easily obtained in crystals. Its molecular weight is 46,000 and its amino acid composition differs from that of serum albumin. Other proteins of egg white are conalbumin, lysozyme, ovoglobulin, ovomucoid, and avidin. Lysozyme is an enzyme that hydrolyzes the carbohydrates found in the capsules certain bacteria secrete around themselves; it causes lysis (disintegration) of the bacteria. The molecular weight of lysozyme is 14,100. Its three-dimensional structure is similar to that of α-lactalbumin, which stimulates the formation of lactose by the enzyme lactose synthetase. Lysozyme has also been found in the urine of patients suffering from leukemia, meningitis, and renal disease.
Avidin is a glycoprotein that combines specifically with biotin, a vitamin. In animals fed large amounts of raw egg white, the action of avidin results in “egg-white injury.” The molecular weight of avidin, which forms a tetramer, is 16,200. Its amino acid sequence is known.
Egg-yolk proteins contain a mixture of lipoproteins and livetins. The latter are similar to serum albumin, α-globulin, and β-globulin. The yolk also contains a phosphoprotein, phosvitin. Phosvitin, which has also been found in fish sperm, has a molecular weight of 40,000 and an unusual amino acid composition; one third of its amino acids are phosphoserine.
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