Quantitative determination of myosin and actin in rabbit skeletal muscle.
The myosin and actin content of muscle tissue and purified myofibrils from rabbit psoas muscle has been determined. Myofibrils were purified using Percoll gradients, which allowed rapid separation from nuclei and connective tissue proteins. Myosin and actin were quantitated by amino acid analysis of the appropriate bands from sodium dodecyl sulfate/polyacrylamide gels. Muscle tissue contained 94 and 619 nmol/g wet weight of myosin and actin, respectively, while myofibrils had 0.82 and 5.37 mumol/g protein. Thus myosin contributed 43% and actin 22% of the myofibril protein mass. The value of 2.5 myosins per 14.3 nm repeat as calculated from these results suggests that thick filament models with mixtures of two and three crossbridges per repeat should be considered.
D000199:Actins / Q000032:analysis*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D009132:Muscles / Q000032:analysis*; D009210:Myofibrils / Q000032:analysis; D009218:Myosins / Q000032:analysis*; D011817:Rabbits
D000199:Actins; D000596:Amino Acids; D009218:Myosins