[Inhibition and stimulation of ATPase activity and the nonenzymatic hydrolysis of ATP in electron histochemistry (author's transl)].
In rat liver, homogenized and fractionated, ATPase activity was studied both histochemically and biochemically in the presence of lead ions and with addition of cysteine, EDTA, 2,4-DNP, sodium cyanide, sodium fluoride and p-chloromercuribenzoate. None of the inhibitors concerned permitted to obtain a complete inhibition of ATP hydrolysis. A practically complete inhibition of ATPase was possible only through heat inactivation or after double prefixation with formaldehyde and ethanol. Nonenzymatic ATP hydrolysis plays a negligible role in ATPase histochemistry since phosphate yield taking place due to lead action is insignificant against enzymatic hydrolysis of ATP.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology / Q000648:ultrastructure; D002467:Cell Nucleus / Q000201:enzymology; D004789:Enzyme Activation / Q000187:drug effects; D004791:Enzyme Inhibitors / Q000494:pharmacology; D000431:Ethanol / Q000494:pharmacology; D005260:Female; D005557:Formaldehyde / Q000494:pharmacology; D006651:Histocytochemistry; D006358:Hot Temperature; D006868:Hydrolysis; D066298:In Vitro Techniques; D008099:Liver / Q000201:enzymology; D008297:Male; D008854:Microscopy, Electron; D008862:Microsomes, Liver / Q000201:enzymology / Q000648:ultrastructure; D008930:Mitochondria, Liver / Q000201:enzymology / Q000648:ultrastructure; D051381:Rats
D004791:Enzyme Inhibitors; D005557:Formaldehyde; D000431:Ethanol; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases
Hemmung und Stimulierung der ATPase-Aktivität und die nichtenzymatische Hydrolyse von ATP in der elektronenmikroskopischen Histochemie