scholarly journals Inhibition studies of alkaline phosphatase in hard tissue-forming cells.

1975 ◽  
Vol 23 (5) ◽  
pp. 342-347 ◽  
Author(s):  
A Linde ◽  
B C Magnusson
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Adenosine Triphosphatase ◽  
Ruthenium Red ◽  
Inorganic Pyrophosphatase ◽  
Alkaline Ph ◽  
Hard Tissue ◽  
Assay Condition ◽  
Phosphatase Inhibitors ◽  
Inhibition Studies

The effects of the alkaline phosphatase inhibitors levamisole and R 8231 on p-nitro-phenylphosphatase, inorganic pyrophosphatase and adenosine triphosphatase (ATPase) activities in dentingenically active odontoblasts were studied. The p-nitrophenylphosphatase and inorganic pyrophosphatase activities were inhibited, while 40% of the ATP-splitting enzyme activity remained under the assay condition used. This finding, togeather with earlier studies, indicates that at least two different phosphatase are active at alkaline pH in hard tissue-forming cells; on nonspecific alkaline phosphatase and one specific ATPase. The ATPase activity is uninfluenced by ouabain and ruthenium red and is activated by Ca-2+ ions.

A Comparison of the Histochemical Enzyme Pattern in Normal and Varicose Veins

1987 ◽  
Vol 2 (3) ◽  
pp. 135-158 ◽  
Author(s):  
Bernhardt Haardt
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Lysosomal Enzymes ◽  
Adenosine Triphosphatase ◽  
Varicose Veins ◽  
Histochemical Demonstration ◽  
Saphenous Veins ◽  
The Media ◽  
Enzyme Pattern

In order to study enzyme activity in the walls of healthy and diseased veins, sections were taken from the stripped varicose long saphenous veins of eight patients. These were subjected to histochemical enzyme investigations. These methods were used to determine levels and localization of lactate dehydrogenase, alkaline phosphatase, adenosine triphosphatase and the lysosomal enzymes, β-glucuronidase, non-specific esterases and acid phosphatase. The method and our findings are described. The results of these histochemical investigations demonstrate an increase in lysosomal enzyme activity in the walls of varicose veins as compared to that of normal veins. This increase is greater in the media than in the intima. Enzymes responsible for energy metabolism demonstrated contradictory behaviour, with decline in the activity of such enzymes in the walls of varicose veins. This decline in enzyme activity was more marked in the intima than in the media and was especially noticeable in the histochemical demonstration of Ca++-adenosine triphosphatase.

EFFECT OF THYROCALCITONIN ON ALKALINE PHOSPHATASE AND PYROPHOSPHATASE IN RAT TIBIA, KIDNEY AND INTESTINE

1972 ◽  
Vol 70 (4) ◽  
pp. 676-682 ◽  
Author(s):  
Cipora Streifler ◽  
Arie Orenstein ◽  
Arieh Harell
Keyword(s):  
Alkaline Phosphatase ◽  
Kidney Tissue ◽  
Plasma Calcium ◽  
Inorganic Pyrophosphatase ◽  
Rat Tibia ◽  
Rat Bone

ABSTRACT The influence of thyrocalcitonin (TCT) on the enzymes alkaline phosphatase and inorganic pyrophosphatase in rat bone, kidney and intestine was studied. The rats were injected with TCT every hour for 4 hours. They were divided into groups and were sacrificed 1 h after the first, second, third and fourth injection respectively. The plasma calcium was found to be reduced. Enzyme studies showed that: a) in tibia metaphysis homogenates alkaline phosphatase increased in response to TCT, to 198, 175, 154 and 183 per cent of the non-injected rats after 1, 2, 3, and 4 injections, respectively; inorganic pyrophosphatase was elevated to 356, 209, 221, 425 per cent after the same TCT injections. b) In kidney homogenates alkaline phosphatase was reduced to 75, 53, 79, 68 per cent of the non-injected rats after 1, 2, 3 and four doses, respectively; inorganic pyrophosphatase was reduced to 78, 56, 77 and 71 per cent after the same injections of TCT. c) In the jejunum, alkaline phosphatase was found to be 88.5, 71, 91 and 115 per cent of the untreated rats after 1, 2, 3 and 4 injections, respectively; pyrophosphatase in this tissue was found to be 105, 102, 102 and 113 per cent of the normal under the above conditions. The results indicate: 1. TCT causes increases in alkaline phosphatase and inorganic pyrophosphatase activities in bone. The increase of pyrophosphatase is significantly more marked than the increase of alkaline phosphatase; 2. in kidney tissue, the action of TCT on these two enzymes is slower and their activities are equally reduced; 3. in the jejunum no significant effect of TCT on the activity of these two enzymes was observed.

scholarly journals Synthesis of new Cadmium(II) Complexes of Schiff Bases as Alkaline Phosphatase Inhibitors and their Antimicrobial Activity

2021 ◽  
pp. 103308
Author(s):  
Rana Muhammad Irfan ◽  
Muhammad Ashraf Shaheen ◽  
Muhammad Saleem ◽  
Muhammad Nawaz Tahir ◽  
Khurram Shahzad Munawar ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Alkaline Phosphatase ◽  
Schiff Bases ◽  
Phosphatase Inhibitors

scholarly journals The cobalt(II)-alkaline phosphatase system at alkaline pH.

1988 ◽  
Vol 263 (23) ◽  
pp. 11263-11268
Author(s):  
L Banci ◽  
I Bertini ◽  
C Luchinat ◽  
M S Viezzoli ◽  
Y J Wang
Keyword(s):  
Alkaline Phosphatase ◽  
Alkaline Ph ◽  
Phosphatase System

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 Increase in alkaline phosphatase activity in calvaria cells cultured with diphosphonates

1979 ◽  
Vol 183 (1) ◽  
pp. 73-81 ◽  
Author(s):  
R Felix ◽  
H Fleisch
Keyword(s):  
Alkaline Phosphatase ◽  
Protein Synthesis ◽  
Enzyme Activity ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Heat Inactivation ◽  
High Concentration ◽  
Control Value ◽  
Km Value ◽  
Inhibitor Of Protein Synthesis

1. Dichloromethanediphosphonate and to a lesser degree 1-hydroxyethane-1,1-diphosphonate, two compounds characterized by a P-C-P bond, increased the alkaline phosphatase activity of cultured rat calvaria cells up to 30 times in a dose-dependent fashion. 2. Both diphosphonates also slightly inhibited the protein synthesis in these cells. 3. Thymidine, an inhibitor of cell division, did not inhibit the induction of the enzyme, indicating that the increase in enzyme activity was not due to the formation of a specific population of cells with high alkaline phosphatase activity. 4. The effect on alkaline phosphatase was suppressed by the addition of cycloheximide, an inhibitor of protein synthesis. 5. After subculturing the stimulated cells in medium without diphosphonates, the enzyme activity fell almost to the control value. 6. Bovine parathyrin diminished the enzyme activity of the control cells and the cells treated with dichloromethanediphosphonate; however, at high concentration the effect of parathyrin was greater on the diphosphonate-treated cells than on the control cells. 7. The electrophoretic behaviour, heat inactivation, inhibition by bromotetramisole or by phenylalanine, and the Km value of the induced enzyme were identical with that of the control enzyme.

SIGNIFICANCE OF TRANSAMINASE ACTIVITY OF SERUM

PEDIATRICS ◽  
1959 ◽  
Vol 24 (3) ◽  
pp. 360-361
Author(s):  
SAMUEL P. BESSMAN
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Transaminase Activity ◽  
Specific Approach ◽  
Normal Tissues ◽  
The Past ◽  
Glycolytic Activity ◽  
Enzyme Characteristic ◽  
Phosphatase Alkaline

THE MEASUREMENT of enzyme activity of serum as an indicator of disease has a long history in medicine. In the past, it has been the aim of the designers of these methods to make them as specific as possible for assay of an enzyme characteristic of a particular system or group of similar organs. Examples of these venerable tests are those for amylase, acid phosphatase, alkaline phosphatase and choline esterase in the serum. Warburg made the first departure from this specificity by demonstrating that the activity of triosephosphate dehydrogenase in the serum of animals with cancer was much greater than that of controls. This test was partially specific, for as Warburg had earlier shown, the glycolytic activity of tumors is much greater than that of normal tissues. The non-specific approach became extreme with the introduction of the measurement of the glutamic-oxalacetic transaminase reaction in the diagnosis of acute coronary disease.

Inorganic Pyrophosphatase Activity of Purified Bovine Pulp Alkaline Phosphatase at Physiological pH

1986 ◽  
Vol 65 (2) ◽  
pp. 125-127 ◽  
Author(s):  
M. Harada ◽  
N. Udagawa ◽  
K. Fukasawa ◽  
B.Y. Hiraoka ◽  
M. Mogi
Keyword(s):  
Alkaline Phosphatase ◽  
Inorganic Pyrophosphatase ◽  
Pyrophosphatase Activity

Acid phosphatase, alkaline phosphatase, and nitrate reductase activity of selected ectomycorrhizal fungi

1989 ◽  
Vol 67 (3) ◽  
pp. 750-753 ◽  
Author(s):  
Iwan Ho
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Nitrate Reductase ◽  
Phosphatase Activity ◽  
Ectomycorrhizal Fungi ◽  
Acid Phosphatase Activity ◽  
Nitrate Reductase Activity ◽  
Reductase Activity ◽  
Phosphatase Alkaline

Seventeen isolates, encompassing five genera and eight species of ectomycorrhizal fungi, were compared for acid phosphatase, alkaline phosphatase, and nitrate reductase activity. Isolates within species differed in enzyme activity and isozyme patterns by host specificity and site (as exemplified by the genus Suillus). Host and site may have affected phosphatase enzyme activity. Generally, the Douglas-fir associates, which dominate in mesic sites, have higher acid phosphatase activity than pine associates, which mostly occupy xeric sites; however, pine associates from mesic sites also have higher acid phosphatase activity (e.g., S. tomentosus). In four isolates of Amanita muscaria, the effect of site was also apparent. Two of them, which have significantly higher acid phosphatase activity than the others, were isolated from mesic sites. The isozyme pattern of the genus Suillus appeared to be separated by host groups. Other isolates with only one species also differed more or less by host groups. They shared at least one band within host groups, except for the two isolates of Paxillus involutus from different hosts. The P. involutus S-403 isolated from an orchard showed much higher nitrate reductase activity than all other isolates. No apparent differences in nitrate reductase activity were found between the other isolates.

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