A combined histochemical and biochemical study of myofibrillar ATPase in pectoral, leg and cardiac muscle of several species of bird.
Frozen sections of the pectoral, gastrocnemius and cardiac muscles from seven different species of birds were stained for myofibrillar ATPase and for succinic dehydrogenase. Several methods of myofibrillar ATPase were used including different pre-incubation treatments. Myofibrillar ATPases were also measured biochemically and the pH profile of the activity was compared with the histochemical staining following pre-incubation at different pH. Myofibrils from the different muscles were also subjected to sodium dodecyl sulphate acrylamide gel electrophoresis in order to separate the low molecular weight components of myosin. The results demonstrated that histochemical methods can be applied, with a reasonable degree of confidence, to classifying fibres in avian muscles although the classification used for mammalian muscles needs to be modified. They also showed that avian muscles, particularly the pectoralis, varies considerably between species and their mode of locomotion.
D000251:Adenosine Triphosphatases / Q000032:analysis* / Q000378:metabolism; D000818:Animals; D001717:Birds / Q000033:anatomy & histology*; D006651:Histocytochemistry; D006863:Hydrogen-Ion Concentration; D009132:Muscles / Q000201:enzymology*; D009206:Myocardium / Q000201:enzymology*; D009210:Myofibrils / Q000201:enzymology; D013045:Species Specificity; D013385:Succinate Dehydrogenase / Q000032:analysis / Q000378:metabolism
D013385:Succinate Dehydrogenase; D000251:Adenosine Triphosphatases