No classical type IIB fibres in dog skeletal muscle.
To analyse the fibre type composition of adult dog skeletal muscle, enzyme histochemistry, immunohistochemistry for type I, IIA and IIB myosins, and peptide mapping of myosin heavy chains isolated from typed single according to the activity of the m-ATPase after acidic and alkaline preincubation proved to be rather difficult and was only consistently achieved after a very careful adjustment of the systems used. One of these sub-classes of type II fibres stained more strongly for m-ATPase activity after acidic and alkaline preincubation, was oxidative-glycolytic and showed a strong reaction with an anti-type IIA myosin. The other one, however, although showed a faint reaction with an anti-type IIB myosin. Peptide mapping of the myosin heavy chains of typed single fibres revealed two populations of heavy chains among the type II fibre group. Thus, in dog muscle, we are confronted with the presence of two main classes of type II fibres, both oxidative-glycolytic, but differing in the structure of their myosin heavy chains. In contrast to some reports in the literature, no classical type IIB fibres could be detected.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D002415:Cats; D004285:Dogs; D006651:Histocytochemistry; D009132:Muscles / Q000166:cytology* / Q000502:physiology; D009218:Myosins / Q000032:analysis / Q000378:metabolism; D010446:Peptide Fragments / Q000032:analysis; D013194:Staining and Labeling
D010446:Peptide Fragments; D000251:Adenosine Triphosphatases; D009218:Myosins