Interactions of Ca, P, Zn, and Alkaline Phosphatase in the Chick. II. Effect of Dietary Ca Level

1974 ◽  
Vol 52 (1) ◽  
pp. 90-95 ◽  
Author(s):  
L. W. McCuaig ◽  
I. Motzok
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Inorganic Phosphate ◽  
Duodenal Mucosa ◽  
Positive Correlation ◽  
Mn Content

Chicks were fed a semi-purified diet, containing 0.75% Ca, 0.5% inorganic phosphate (Pi), and 50 p.p.m. Zn, to 2 weeks of age. They were then divided into groups and fed the same diet with 0, 0.75, 1.50, 2.25, or 3.00% Ca, for 4 or 7 days before being killed. Plasma was analyzed for Ca, Pi, and Zn, and duodenal mucosa for Ca, Pi, Zn, Mn, and alkaline phosphatase (AP). The low Ca treatment decreased plasma and mucosa Ca and increased mucosa Zn, whereas the high Ca diets increased mucosa Ca and decreased mucosa Zn, plasma Pi, and mucosa AP activity. There was an overall positive correlation of AP with plasma and mucosa Zn, and plasma and mucosa Pi, and a negative overall correlation of AP with plasma and mucosa Ca. Mucosa Mn content did not seem to be related to the enzyme activity.

ELECTRON MICROSCOPY OF ALKALINE PHOSPHATASE OF ESCHERICHIA COLI

1966 ◽  
Vol 12 (4) ◽  
pp. 605-607 ◽  
Author(s):  
V. M. Kushnarev ◽  
T. A. Smirnova
Keyword(s):  
Electron Microscopy ◽  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Cell Wall ◽  
Enzyme Activity ◽  
Electron Microscope ◽  
Inorganic Phosphate ◽  
E Coli

A method is described for determining the localization of alkaline phosphatase in the cells of E. coli B with the electron microscope. Enzyme activity, determined by deposition of inorganic phosphate, is located in the exterior layer of the cell wall.

Automated Determination of Serum Alkaline Phosphatase Using a Modified Bodansky Technic

1964 ◽  
Vol 10 (1) ◽  
pp. 75-82 ◽  
Author(s):  
H Keay ◽  
J A Trew
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Inorganic Phosphate ◽  
Serum Alkaline Phosphatase ◽  
Automated Determination

Abstract An automated procedure for the measurement of alkaline phosphatase activity by a modification of the Bodansky method is described. It has been possible to adapt the Fiske-SubbaRow method for phosphate so that alkaline phosphatase is determined by a second run, immediately following the determination of inorganic phosphate. Studies of the effect of time, pH, and concentration of barbital on the enzyme activity are discussed, and the advantages of the method are listed.

Regulation of Intestinal Alkaline Phosphatase by Dietary Phosphate

1972 ◽  
Vol 50 (12) ◽  
pp. 1152-1156 ◽  
Author(s):  
L. W. McCuaig ◽  
I. Motzok
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Enzyme Activities ◽  
Inorganic Phosphate ◽  
Intestinal Alkaline Phosphatase ◽  
Dietary Phosphate ◽  
Intestinal Enzyme

Day-old chicks were fed practical rations containing varying levels of inorganic phosphate (Pi) in an attempt to study the regulation of intestinal alkaline phosphatase by phosphate. Low dietary Pi (0.16%) increased the enzyme activity by 50% compared to adequate Pi (0.48%). The enzyme activities were significantly reversed 8 days after reversing the diets. In another experiment chicks were fed 0.16 or 0.80%) Pi for 4 weeks and killed when full-fed, or after 3 days' starvation. In the full-fed birds low dietary Pi reduced the intestinal nuclear Pi and doubled the intestinal enzyme activity. Nuclear Pi was found to be inversely correlated with alkaline phosphatase in the fed animals. No such effects were found in the starved birds.

Enzyme activity of zhargalant farm soil, central province of Mongolia

2018 ◽  
Vol 22 (03) ◽  
pp. 109-113
Author(s):  
Bayarmaa J ◽  
Purev D
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Central Province ◽  
Phosphatase Activities ◽  
Positive Correlation ◽  
Wheat Field ◽  
Field Soils

We conducted monitoring analysis of cellulase, saccharase, protease, urease, acid and alcaline phosphatase activities of Zhargalant farm soil, Central province of Mongolia. From the results it is clear seen that for the year activity of cellulase, protease and urease are increased but activity of saccharase decreased. The activity of acid phosphatase on control, wheat and nearby wheat field soils decreased but on rape and nearby rape fields its activity increased. About alkaline phosphatase its activity decreased on control and soil of wheat field, on soils of nearby wheat, rape and nearby rape fields its activity increased. For the field where seeding crops did not produces there was positive correlation between humus and enzyme activity, but for the soils were the crops were sown this correlation changes depending on the enzymes. This trend is also observed for the soils of nearby fields.

scholarly journals THE ESTIMATION OF SERUM INORGANIC PHOSPHATE AND "ACID" AND "ALKALINE" PHOSPHATASE ACTIVITY

1942 ◽  
Vol 142 (2) ◽  
pp. 921-933 ◽  
Author(s):  
George Y. Shinowara ◽  
Lois M. Jones ◽  
Harry L. Reinhart
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Inorganic Phosphate ◽  
Acid And Alkaline Phosphatase ◽  
Serum Inorganic Phosphate

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.

Effect of Age on Oxygen-Binding in Normal Human Subjects

1976 ◽  
Vol 51 (2) ◽  
pp. 185-188
Author(s):  
P. M. Tweeddale ◽  
R. J. E. Leggett ◽  
D. C. Flenley
Keyword(s):  
Oxygen Saturation ◽  
Oxygen Tension ◽  
Inorganic Phosphate ◽  
Human Subjects ◽  
Oxygen Binding ◽  
Corpuscular Haemoglobin ◽  
Positive Correlation ◽  
Normal Human ◽  
Mean Corpuscular Haemoglobin ◽  
Effect Of Age

1. Oxygen-binding, plasma and intra-erythrocytic pH, and haemoglobin, 2,3-diphosphoglycerate and inorganic phosphate concentrations were measured in sixty-two healthy non-smokers aged between 18 and 89 years. 2. P50 (oxygen tension at 50% oxygen saturation) expressed at plasma pH 7·40 and Pco2 5·33 kPa showed a positive correlation with age. 3. This correlation of P50 with age was closer when P50 was expressed at a constant intra-erythrocytic pH 7·20. On average P50 at intra-erythrocytic pH 7·20 increased from 3·59 kPa at 20 years to 3·96 kPa at 90 years of age. 4. 2,3-Diphosphoglycerate, inorganic phosphate, haemoglobin and mean corpuscular haemoglobin concentrations did not correlate with P50 or with age.

Binding of 3-phosphoglycerate leads to both activation and stabilisation of ADP-glucose pyrophosphorylase from apple leaves

2005 ◽  
Vol 32 (9) ◽  
pp. 839
Author(s):  
Rui Zhou ◽  
Lailiang Cheng
Keyword(s):  
Heat Treatment ◽  
Thermal Stability ◽  
Enzyme Activity ◽  
Inorganic Phosphate ◽  
Thermal Inactivation ◽  
Specific Activity ◽  
Apple Leaves ◽  
Apparent Homogeneity ◽  
Adp Glucose Pyrophosphorylase ◽  
High Concentrations

Apple leaf ADP-glucose pyrophosphorylase was purified 1436-fold to apparent homogeneity with a specific activity of 58.9 units mg–1. The enzyme was activated by 3-phosphoglycerate (PGA) and inhibited by inorganic phosphate (Pi) in the ADPG synthesis direction. In the pyrophosphorolytic direction, however, high concentrations of PGA (> 2.5 mm) inhibited the enzyme activity. The enzyme was resistant to thermal inactivation with a T0.5 (temperature at which 50% of the enzyme activity is lost after 5 min incubation) of 52°C. Incubation with 2 mm PGA or 2 mm Pi increased T0.5 to 68°C. Incubation with 2 mm dithiothreitol (DTT) decreased T0.5 to 42°C, whereas inclusion of 2 mm PGA in the DTT incubation maintained T0.5 at 52°C. DTT-induced decrease in thermal stability was accompanied by monomerisation of the small subunits. Presence of PGA in the DTT incubation did not alter the monomerisation of the small subunits of the enzyme induced by DTT. These findings indicate that binding of PGA renders apple leaf AGPase with a conformation that is not only more efficient in catalysis but also more stable to heat treatment. The physiological significance of the protective effect of PGA on thermal inactivation of AGPase is discussed.

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.

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