Category: Proteins

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…

Milk contains the following: an albumin, α-lactalbumin; a globulin, beta-lactoglobulin; and a phosphoprotein, casein. If acid is added to milk, casein precipitates. The remaining watery liquid (the supernatant solution), or whey, contains α-lactalbumin and β-lactoglobulin. Both have been obtained in crystalline form; in bovine milk, their molecular weights are approximately 14,000 and 18,400, respectively. Lactoglobulin also occurs as a dimer of…

Human blood serum contains about 7 percent protein, two-thirds of which is in the albumin fraction; the other third is in the globulin fraction. Electrophoresis of serum reveals a large albumin peak and three smaller globulin peaks, the alpha-, beta-, and gamma-globulins. The amounts of alpha-, beta-, and gamma-globulin in normal human serum are approximately 1.5, 1.9, and 1.1 percent, respectively. Each globulin fraction is a mixture of…

Fibrinogen, the protein of the blood plasma, is converted into the insoluble protein fibrin during the clotting process. The fibrinogen-free fluid obtained after removal of the clot, called blood serum, is blood plasma minus fibrinogen. The fibrinogen content of the blood plasma is 0.2 to 0.4 percent. Fibrinogen can be precipitated from the blood plasma by half-saturation with sodium chloride. Fibrinogen solutions…

The total amount of muscle proteins in mammals, including humans, exceeds that of any other protein. About 40 percent of the body weight of a healthy human adult weighing about 70 kilograms (150 pounds) is muscle, which is composed of about 20 percent muscle protein. Thus, the human body contains about 5 to 6 kilograms (11 to 13 pounds) of muscle…

Keratin, the structural protein of epithelial cells in the outermost layers of the skin, has been isolated from hair, nails, hoofs, and feathers. Keratin is completely insoluble in cold or hot water; it is not attacked by proteolytic enzymes (i.e., enzymes that break apart, or lyse, protein molecules), and therefore cannot replace proteins in the diet. The…

Scleroproteins Collagen Collagen is the structural protein of bones, tendons, ligaments, and skin. For many years collagen was considered to be insoluble in water. Part of the collagen of calf skin, however, can be extracted with citrate buffer at pH 3.7. A precursor of collagen called procollagen is converted in the body into collagen. Procollagen has a molecular weight of 120,000. Cleavage of one…

Despite its weaknesses, a functional classification is used here in order to demonstrate, whenever possible, the correlation between the structure and function of a protein. The structural, fibrous proteins are presented first, because their structure is simpler than that of the globular proteins and more clearly related to their function, which is the maintenance of…

In view of the unsatisfactory state of the old classification, it is preferable to classify the proteins according to their biological function. Such a classification is far from ideal, however, because one protein can have more than one function. The contractile protein myosin, for example, also acts as an ATPase (adenosine triphosphatase), an enzyme that hydrolyzes adenosine triphosphate (removes…

When a solution of a protein is boiled, the protein frequently becomes insoluble—i.e., it is denatured—and remains insoluble even when the solution is cooled. The denaturation of the proteins of egg white by heat—as when boiling an egg—is an example of irreversible denaturation. The denatured protein has the same primary structure as the original, or native, protein.…