LEAD-ADENOSINE TRIPHOSPHATE COMPLEXES IN ADENOSINE TRIPHOSPHATASE HISTOCHEMISTRY
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چکیده
منابع مشابه
Studies on Myofibrillar Adenosine Triphosphatase with Calcium-free Adenosine Triphosphate.
It has been reported by several groups of workers that incubation of the relaxing factor granar of muscle with magnesium and adenosine triphosphate results in the formation of a soluble relaxing substance capable of inhibiting the magnesium-activated adenosine triphosphatase activity of myofibrils or actomyosin (3-6) and the contraction of single glycerinated muscle fibers (7). In addition, Uri...
متن کاملSynthesis of adenosine triphosphate and exchange between inorganic phosphate and adenosine triphosphate in sodium and potassium ion transport adenosine triphosphatase.
Radioactive adenosine triphosphate was synthesized transiently from adenosine diphosphate and radioactive inorganic phosphate by sodium and potassium adenosine triphosphatase from guinea pig kidney. In a first step, K+-sensitive phosphoenzyme was formed from radioactive inorganic phosphate in the presence of magnesium ion and 16 mM sodium ion. In a second step the addition to the phosphoenzyme ...
متن کاملActivation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase.
The steady state kinetics of sodium and potassium ion transport adenosine triphosphatase (EC 3.6-l. 3) suggests an activating action of adenosine triphosphate in addition to its action as a phosphate donor. This action might be an acceleration of dissociation of Kf or its congeners from the enzyme. To test this possibility transient kinetics of the phosphoenzyme was investigated. In membranes f...
متن کاملBinding of adenosine triphosphate to sodium and potassium ion-stimulated adenosine triphosphatase.
In order to characterize a step in the reaction sequence of sodium and potassium ion-dependent adenosine triphosphatase (EC 3.6.1.3), the binding of radioactive adenosine triphosphate to kidney cell membranes was estimated by flow dialysis in the presence of a chelator of divalent cations, which prevented hydrolysis of the adenosine triphosphate. Adenosine triphosphate was bound to a single sit...
متن کاملThe rate-limiting step of the protamine-induced adenosine triphosphatase activity of adenosine triphosphate-G-actin.
The release of Pi from the Pi-G-actin-ADP complex is the rate-limiting step in the ATPase activity that is shown by ATP-G-actin in the presence of protamine.
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ژورنال
عنوان ژورنال: Journal of Histochemistry & Cytochemistry
سال: 1969
ISSN: 0022-1554,1551-5044
DOI: 10.1177/17.2.85