LEAD-ADENOSINE TRIPHOSPHATE COMPLEXES IN ADENOSINE TRIPHOSPHATASE HISTOCHEMISTRY
Open Access
- 1 February 1969
- journal article
- research article
- Published by SAGE Publications in Journal of Histochemistry & Cytochemistry
- Vol. 17 (2) , 85-94
- https://doi.org/10.1177/17.2.85
Abstract
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.Keywords
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