Abstract
Adult human muscle in tissue culture gives rise to myotubes which show strong NADH-TR activity, weak phosphorylase activity, strong myosin ATPase activity, and moderate levels of PAS-positive material. No “fibre types” were observed. No difference could be detected in the histochemical profile of myotubes derived from control and diseased muscle in culture. It is possible that histochemical abnormalities in cultured human muscle may only be observed when innervated and therefore more fully differentiated. Embryonic chick muscle in culture gives myotubes that have strong phosphorylase activity, moderate NADH-TR activity, strong myosin ATPase activity and moderate levels of PAS-positive material, suggesting species-specific determinants of enzymatic differentiation.
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