pH lability of myosin ATPase activity permits discrimination of different muscle fibre types in crustaceans.
Myofibrillar actomyosin ATPase activity has been studied histochemically in the closer muscle of the crab Eriphia spinifrons. Preincubation at pH 4.6 and 5.0 reveals differences in the lability of the ATPase. This permits the discrimination of four fibre types. Of these, three represent subgroups of rapidly contracting fibres. The histochemically defined fibre types correspond well with four groups defined according to electrophysiological criteria.
D000205:Actomyosin / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D003386:Brachyura / Q000502:physiology*; D005071:Evoked Potentials; D006651:Histocytochemistry; D006863:Hydrogen-Ion Concentration; D009132:Muscles / Q000201:enzymology* / Q000502:physiology; D009210:Myofibrils / Q000201:enzymology* / Q000502:physiology
D000205:Actomyosin; D000251:Adenosine Triphosphatases