scholarly journals LEAD ION AND PHOSPHATASE HISTOCHEMISTRY III. THE EFFECTS OF LEAD AND ADENOSINE TRIPHOSPHATE CONCENTRATION ON THE INCORPORATION OF PHOSPHATE INTO FIXED TISSUE

1969 ◽  
Vol 17 (9) ◽  
pp. 608-612 ◽  
Author(s):  
ALAN S. ROSENTHAL ◽  
HAROLD L. MOSES ◽  
LOIS TICE ◽  
CHARLES E. GANOTE
Keyword(s):  
Enzyme Activity ◽  
Adenosine Triphosphate ◽  
Adenosine Triphosphatase ◽  
Lead Nitrate ◽  
Lead Ion ◽  
Fixed Tissue ◽  
Phosphate Release ◽  
Adenosine Triphosphatase Activity ◽  
High Lead

This communication attempts to separate and define the relationships between lead inhibition of tissue adenosine triphosphatase activity, lead. catalyzed adenosine triphosphate hydrolysis and reaction product localization when the Wachstein-Meisel reaction is applied to kidney. Using a radiochemical assay of adenosine triphosphatase activity and varying the concentration of lead nitrate or adenosine triphosphate, the quantity of phosphate bound to and released from tissue was determined. Depending on the relative concentrations of lead and adenosine triphosphate, two situations may exist. With low lead or high adenosine triphosphate concentrations, phosphate release by tissue exceeds phosphate trapped by tissue and substantial quantities of phosphate are lost to the medium. With low adenosine triphosphate or high lead concentrations more phosphate is bound in tissue than can be attributed to tissue enzyme activity. Possible explanations for these phenomenon are discussed.

scholarly journals LEAD ION AND PHOSPHATASE HISTOCHEMISTRY II. EFFECT OF ADENOSINE TRIPHOSPHATE HYDROLYSIS BY LEAD ION ON THE HISTOCHEMICAL LOCALIZATION OF ADENOSINE TRIPHOSPHATASE ACTIVITY

1966 ◽  
Vol 14 (10) ◽  
pp. 702-710 ◽  
Author(s):  
HAROLD L. MOSES ◽  
ALAN S. ROSENTHAL ◽  
DAVID L. BEAVER ◽  
SHIRLEY S. SCHUFFMAN
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Lead Nitrate ◽  
Histochemical Localization ◽  
Lead Ion ◽  
Membrane Localization ◽  
Fixed Tissue ◽  
Plasma Membrane Localization ◽  
Hydrolysis Of

The lead method of Wachstein and Meisel for the histochemical localization of adenosine triphosphatase (ATPase) involves the incubation of sections of fixed tissue in reaction mixtures containing ATP, lead nitrate, magnesium sulfate and a Tris-maleate buffer, pH 7.2. Both fixation and the presence of lead ion were shown to inhibit tissue ATPase activity markedly and to inactivate the sodium- plus potassium-dependent membrane ATPase. In addition, recent studies have demonstrated that lead ion, in the concentration used in the Wachstein-Meisel system, will catalyze the hydrolysis of ATP. Studies on the effect of this nonenzymatic reaction on the histochemical localization of ATPases demonstrated that plasma membrane localization occurred only with lead and ATP concentrations which gave significant nonenzymatic hydrolysis of ATP by lead. In addition, nuclear and mitochondrial localization without accompanying plasma membrane localization could be obtained in formalin-fixed tissue with decreased concentrations of lead or with increased concentrations of ATP in the reaction mixture. The amount of lead-catalyzed hydrolysis was in the same order of magnitude as fixed tissue ATPase activity and could quantitatively account for the amount of phosphate needed to give recognizable localization of lead salt deposits in sections of fixed tissue.

scholarly journals ULTRASTRUCTURAL LOCALIZATION OF Mg++-DEPENDENT DINITROPHENOL-STIMULATED ADENOSINE TRIPHOSPHATASE IN HUMAN BLOOD PLATELETS

1967 ◽  
Vol 15 (5) ◽  
pp. 267-272 ◽  
Author(s):  
VICTOR G. VETHAMANY ◽  
SYDNEY S. LAZARUS
Keyword(s):  
Enzyme Activity ◽  
Plasma Membrane ◽  
Human Blood ◽  
Adenosine Triphosphatase ◽  
Blood Platelets ◽  
Ultrastructural Localization ◽  
Human Platelets ◽  
Structural Localization ◽  
Adenosine Triphosphatase Activity ◽  
Human Blood Platelets

Fine structural localization of adenosine triphosphatase activity was studied in human platelets briefly fixed in cold formol calcium and then incubated in lead medium with added dinitrophenol. Under these conditions, the Mg++-dependent dinitrophenol-stimulated adenosine triphosphatase of platelet mitochondria was demonstrated, but neither granules nor plasma membrane showed enzyme activity.

scholarly journals An active-site-directed adenosine triphosphate analogue binds to the β-subunits of factor F1 mitochondrial adenosine triphosphatase with its triphosphate moiety

1979 ◽  
Vol 182 (2) ◽  
pp. 617-619 ◽  
Author(s):  
V L Drutsa ◽  
I A Kozlov ◽  
Y M Milgrom ◽  
Z A Shabarova ◽  
N I Sokolova
Keyword(s):  
Adenosine Triphosphate ◽  
Sodium Dodecyl Sulphate ◽  
Active Site ◽  
Adenosine Triphosphatase ◽  
Covalent Binding ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Beta Subunit ◽  
Mixed Anhydride ◽  
Adenosine Triphosphatase Activity

The reaction of the mixed anhydride of [3H]ATP and mesitylenecarboxylic acid and soluble mitochondrial adenosine triphosphatase is accompanied by the covalent binding of one molecule of the inhibitor to a molecule of the enzyme and results in the inhibition of adenosine triphosphatase activity by more than 90%. The electrophoresis of adenosine triphosphatase modified by reaction with the mixed anhydride of [3H]ATP and mesitylenecarboxylic acid in polyacrylamide gel in the presence of sodium dodecyl sulphate showed that the inhibitor is bound to the beta-subunit of the enzyme. The results suggest that ATP may also bind to the beta-subunit of the adenosine triphosphatase with its triphosphate moiety.

scholarly journals Some Factors Involved in the Effect of X-Irradiation on the Phosphatase Activity of Hematopoietic Tissues

Blood ◽  
1959 ◽  
Vol 14 (10) ◽  
pp. 1128-1136 ◽  
Author(s):  
EDWIN M. UYEKI ◽  
PAUL R. SALERNO
Keyword(s):  
Bone Marrow ◽  
Enzyme Activity ◽  
Peripheral Blood ◽  
Adenosine Triphosphatase ◽  
Lymphoid Tissues ◽  
X Ray ◽  
Adenosine Triphosphatase Activity ◽  
Assay Medium ◽  
X Irradiation ◽  
Total Body

Abstract Factors which modify lymphoid distribution of tissues were found to modify the adenosine triphosphatase activity of these tissues. Starvation or cortisone injection, which produces destructive changes in lymphoid tissues, was found to increase the enzyme activity of spleen and thymus tissues. The greater increment of enzyme activity of the thymus as compared to that of the spleen was correlated with its normally higher content of lymphoid tissue. The increase in adenosine triphosphatase activity of hematopoietic tissues appears to be associated with the type of cells present in the assay medium. With respect to peripheral blood leukocytes of the rat, the cell type is confined largely to lymphocytes and granulocytes. The increase in adenosine triphosphatase activity of the leukocytes after total-body x-ray was seen to parallel the increase in granulocytes present in the assay medium. The ratio of granulocytes to lymphocytes is not appreciably altered in dog peripheral blood after exposure to total-body x-ray; the adenosine triphosphatase activity similarly was not significantly altered. After total-body x-ray (390 r and 780 r), cells isolated from the rat bone marrow displayed a fivefold increase in adenosine triphosphatase activity. This increase was seen to correspond with an increase in the ratio of segmented leukocytes and reticuloendothelial cells and a decrease in the immature forms of the erythroid and myeloid cells. The heterogeneous cell mixtures used for our assay procedures permit the observation that total-body x-irradiation results in an increased enzyme activity of the isolated cells of the peripheral blood, bone marrow and spleen tissue of the rat. The increased enzyme activity was associated with the increased ratio of cells with high enzyme activity present in the assay medium.

scholarly journals THE HISTOCHEMICAL DEMONSTRATION OF ADENOSINE TRIPHOSPHATASE ACTIVITY IN MYOCARDIUM

1964 ◽  
Vol 12 (10) ◽  
pp. 740-743 ◽  
Author(s):  
N. R. NILES ◽  
J. CHAYEN ◽  
G. J. CUNNINGHAM ◽  
LUCILLE BITENSKY
Keyword(s):  
Enzymatic Activity ◽  
Adenosine Triphosphate ◽  
Adenosine Triphosphatase ◽  
Inhibitory Effect ◽  
Histochemical Demonstration ◽  
Human Myocardium ◽  
Phosphate Esters ◽  
Precise Localization ◽  
Adenosine Triphosphatase Activity

Adenosine triphosphatase has been demonstrated histochemically in rat and human myocardium. To obtain its precise localization in discrete bands, apparently corresponding to the concentration of myosin, it was necessary to modify the existing technique to obtain better preservation of unfixed tissue and maximal enzymatic activity. Thus it was necessary to increase the concentration of calcium and to effect the reaction at pH 9.4 after treatment with 2:4-dinitrophenol. The specificity of the reaction was shown by these factors, by testing with phosphate esters other than adenosine triphosphate, and by the inhibitory effect of magnesium.

scholarly journals The rate-limiting step of the protamine-induced adenosine triphosphatase activity of adenosine triphosphate-G-actin

1979 ◽  
Vol 183 (2) ◽  
pp. 475-476 ◽  
Author(s):  
A Ferri ◽  
E Magri ◽  
E Grazi
Keyword(s):  
Atpase Activity ◽  
Adenosine Triphosphate ◽  
Adenosine Triphosphatase ◽  
Adenosine Triphosphatase Activity ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Rate Limiting

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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