A new histochemical method for magnesium actomyosin adenosine triphosphatase at physiological pH.
A new lead-precipitation technique for demonstrating magnesium-activated actomyosin adenosine triphosphatase (ATPase) at physiological pH and electrolyte levels in fixed skeletal muscle sections is reported. This method is compared with standard acid- and alkali-denatured muscle stained for calcium myosin ATPase as well as calcium-formalin denatured and pyrophosphate-formalin denatured muscle also stained for calcium myosin ATPase. The technique was developed using hamster skeletal muscle; however, it has also been applied to human, rat, and cat muscle. The fiber-type staining intensities of the formalin-denatured magnesium actomyosin ATPase closely resemble those of the formalin-denatured calcium myosin ATPase in rodents, but intensities in Type 1 fibers are reversed relative to calcium myosin ATPase in human muscle. Cat muscle shows intermediate characteristics.
D000205:Actomyosin / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase / Q000378:metabolism*; D000252:Calcium-Transporting ATPases / Q000378:metabolism; D002415:Cats; D006224:Cricetinae; D005404:Fixatives; D006651:Histocytochemistry / Q000379:methods; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007854:Lead / Q000378:metabolism; D009132:Muscles / Q000201:enzymology*; D051381:Rats
D005404:Fixatives; D007854:Lead; D000255:Adenosine Triphosphate; D000205:Actomyosin; D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases