LEAD-ADENOSINE TRIPHOSPHATE COMPLEXES IN ADENOSINE TRIPHOSPHATASE HISTOCHEMISTRY | Zendy

Lois W. Tice | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

LEAD-ADENOSINE TRIPHOSPHATE COMPLEXES IN ADENOSINE TRIPHOSPHATASE HISTOCHEMISTRY

Author(s) -

Lois W. Tice

Publication year - 1969

Publication title -

journal of histochemistry and cytochemistry

Language(s) - English

Resource type - Journals

eISSN - 1551-5044

pISSN - 0022-1554

DOI - 10.1177/17.2.85

Subject(s) - adenosine triphosphate , adenosine triphosphatase , chemistry , chelation , adenosine , enzyme , triphosphatase , biochemistry , microsome , atpase , inorganic chemistry

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 10 4 . 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(NO 3 ) 2 , substrate inhibition disappeared and increased MgCl 2 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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research