LEAD ION AND PHOSPHATASE HISTOCHEMISTRY I. NONENZYMATIC HYDROLYSIS OF NUCLEOSIDE PHOSPHATES BY LEAD ION | Zendy

Alan S. Rosenthal | Zendy; Harold L. Moses | Zendy; David L. Beaver | Zendy; Shirley S. Schuffman | Zendy

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LEAD ION AND PHOSPHATASE HISTOCHEMISTRY I. NONENZYMATIC HYDROLYSIS OF NUCLEOSIDE PHOSPHATES BY LEAD ION

Author(s) -

Alan S. Rosenthal,

Harold L. Moses,

David L. Beaver,

Shirley S. Schuffman

Publication year - 1966

Publication title -

journal of histochemistry and cytochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.971

H-Index - 124

eISSN - 1551-5044

pISSN - 0022-1554

DOI - 10.1177/14.10.698

Subject(s) - chemistry , nucleoside , hydrolysis , nucleoside triphosphate , adenosine triphosphate , phosphatase , phosphate , nucleoside diphosphate kinase , polyphosphate , atp hydrolysis , inorganic chemistry , biochemistry , nucleotide , enzyme , atpase , gene

A previously undescribed catalytic action of lead ion on the nonenzymatic hydrolysis of nucleoside phosphates has been demonstrated. Lead ion (3.6 mM) hydrolyzed adenosine triphosphate (ATP) at pH 7.2 and 37°C. The presence of magnesium and imidazole was stimulatory. The rate appeared to increase with temperature from 25-60°C. The reaction was inhibited by ethylenediaminetetraacetate. Other nucleoside phosphates were hydrolyzed, some less rapidly than ATP. Adenosine triphosphate in the presence of a rate-limiting amount of lead acted as an inhibitor at high concentrations. With a rate-limiting concentration of ATP (0.72 mM), increasing concentrations of lead ion above 0.36 mM catalyzed a linear increase in ATP hydrolysis. It is suggested that this reaction may be a source of artifact in the lead salt method for the histochemical localization of nucleoside phosphatases.

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