Comparison of actomyosin and myosin from rat muscles with marked differences in the ratio of fast oxidative glycolytic and fast glycolytic muscle fibres.
Actomyosin and myosin were isolated from rat fast muscles, differing in the percentage of fast oxidative glycolytic and fast glycolytic fibres. The dependence of actomyosin ATPase activity from these muscles on the pH corresponds to the previously found dependence of myofibrillar ATPase on the pH, followed histochemically. The myosins isolated from the tensor fascia latae muscle (fast glycolytic) and extensor digitorum longus and tibialis anterior muscles (predominantly fast oxidative glycolytic muscles) differ in the effect of mild acid pre-incubation on myosin ATPase activity. They do not contain the same amount of LC3 and also tryptic peptides of these myosins display a slightly different pattern, as revealed by SDS gel electrophoresis.
D000205:Actomyosin / Q000378:metabolism*; D000818:Animals; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D006019:Glycolysis; D006863:Hydrogen-Ion Concentration; D009132:Muscles / Q000032:analysis*; D009218:Myosins / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats
D000205:Actomyosin; D009218:Myosins; D000252:Calcium-Transporting ATPases