Demonstration of activity for alkaline muscle ATPase in polyacrylamide gels using metal conversion methods

ATPase activity from skeletal muscle was tested at pH 9.2 in polyacrylamide gels using cobalt or lead conversion techniques. With cobalt it seems that the ion is precipitated both to acrylamide and to certain muscle components resulting in a reproducible but non‐enzymatic banding pattern. With the lead technique a specific strongly coloured band is present near the cathode. The band is suppressed by p‐hydroxymercuribenzoate but not by levamisole.