
doi: 10.1177/17.2.85
pmid: 4237066
Chelation of lead by adenosine triphosphate (ATP) and its consequences for adenosine triphosphatase histochemistry were examined. The formation constant of lead-ATP chelates was found by two methods to be 4.6-4.7 x 104. The characteristics of enzyme inhibition by lead were consistent with the predicted effects of lead-ATP chelation. Inhibition was overcome by increasing ATP concentrations. With the adenosine triphosphatase from liver microsomes, which retained some activity in the presence of 4 mM Pb(NO3)2, substrate inhibition disappeared and increased MgCl2 was required for optimal activity. Increased solubility of lead phosphate was observed in the presence of increasing quantities of ATP in a manner predictable from lead-ATP chelation.
Adenosine Triphosphatases, Ions, Histocytochemistry, Guinea Pigs, Hydrogen-Ion Concentration, In Vitro Techniques, Kidney, Phosphates, Rats, Kinetics, Adenosine Triphosphate, Lead, Liver, Microsomes, Animals, Calcium, Magnesium
Adenosine Triphosphatases, Ions, Histocytochemistry, Guinea Pigs, Hydrogen-Ion Concentration, In Vitro Techniques, Kidney, Phosphates, Rats, Kinetics, Adenosine Triphosphate, Lead, Liver, Microsomes, Animals, Calcium, Magnesium
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