Determination of myofibrillar and connective tissue protein contents of young and adult avian (Gallus domesticus) skeletal muscles and the N tau-methylhistidine content of avian actins

The myosin, actin, and collagen contents of young and adult avian red (leg) and white (breast) skeletal muscles from White Leghorn chickens have been determined by the use of analytical chromatographic methods developed to quantify the unique amino acids that occur in these proteins. Because one mole of actin purified from the red and white muscles of Leghorn chickens and one mole of myosin contain respectively one and two moles of N tau-methylhistidine, and the molar ratio of myosin and actin in skeletal muscle is known to be 1:6, the myofibrillar myosin and actin contents of avian skeletal muscles can be determined from the amounts of protein-bound N tau-methylhistidine found in acid hydrolysates of this tissue. Actin accounts for an estimated 11.2 to 12.2% of total muscle mass in both muscles or about 21.1% of total myofibrillar protein, whereas myosin ranges from 23.4 to 25.8% of total protein, corresponding to a mean value of 43.8% of total myofibrillar proteins. Total avian collagen ranged from 1.96 to 3.08% in breast and from 5.63 to 6.87% in leg skeletal muscles. With the methods described herein, content of collagen and collagen-like proteins can be calculated from amounts of 5-hydroxylysine present. The content of total connective tissue proteins could also be calculated from amounts of 4-hydroxyproline found. These quantifications are based on total protein content of the selected avian muscles determined by their detailed amino acid composition.