Cytochemical Studies on the Embryonic Development of Drosophila melanogaster

1950 ◽  
Vol s3-91 (13) ◽  
pp. 79-88
Author(s):  
T. YAO
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Strong Acid ◽  
Mature Oocyte ◽  
Drosophila Embryo ◽  
Centre Of Origin ◽  
Embryonic Life ◽  
Striking Change

1. Drosophila ovary and testis are very rich in acid phosphatase, but contain no histochemical trace of alkaline phosphatase. Thus the mature oocyte shows a strong acid phosphatase reaction both in the nucleus and cytoplasm. Sperm heads are equally reactive. 2. Acid phosphatase is demonstrable in Drosophila embryos from early cleavage up t6 the hatched larva. No striking change in enzyme activity has been observed during this period. 3. Alkaline phosphatase is not detectable in the first half of embryonic life. It suddenly appears in the ventral ectoderm near the future thorax during or shortly after the contraction of the germ band. The enzyme activity then spreads to the other parts of the embryo following definite patterns, until finally the whole embryo becomes active. The possible mechanism of the spreading of enzyme activity is discussed. 4. Alkaline phosphatase disappears in most tissues before hatching, but is retained in the gut epithelia, salivary glands, and Malpighian tubes. The relationship of this enzyme to histo-differentiation is suggested. 5. The centre of origin of alkaline phosphatase activity is considered as the ‘differentiation centre’ of the Drosophila embryo. 6. The high cytoplasmic acid phosphatase activity of the oocyte and nurse cells and a similar activity of the yolk in the developing embryos indicate that the enzyme plays some role both in the synthesis and in the degradation of yolk.

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.

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.

scholarly journals The effect of different copper doses and organic fertilisation on soil’s enzymatic activity

2020 ◽  
Vol 66 (No. 2) ◽  
pp. 93-98
Author(s):  
Beata Kuziemska ◽  
Andrzej Wysokiński ◽  
Joanna Trębicka
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Enzymatic Activity ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Organic Materials ◽  
Chicken Manure ◽  
Test Plant ◽  
Orchard Grass ◽  
Organic Fertilisation

A three-year pot experiment carried out in the vegetation hall in 2014–2016 included studying the enzymatic activity of soil, into which various amounts of copper: (100, 200 and 300 mg Cu/kg soil) and organic materials (cattle manure, chicken manure, post-mushroom substrate) were introduced, used separately, at a soil-introduction dose of 2 g C<sub>org</sub>/kg. Copper and organic materials were used once, only in the first year of the study, before sowing test plant orchard grass. In soil collected after the last (fourth) swath of grass in each year of the study, the activity of urease, dehydrogenases, acid, and alkaline phosphatase was determined. Applications of copper to the soil, regardless of its dose, resulted in a decrease in urease, dehydrogenases and alkaline phosphatase and an increase in acid phosphatase activity. The inactivating effect of this metal on the activity of urease, dehydrogenases and alkaline phosphatase increased with the increase of its dose. Organic fertilisation generally increased the enzymatic activity of the analysed soil. In subsequent years of the study, urease and alkaline phosphatase activity decreased, while acid phosphatase activity increased. Dehydrogenase activity did not change significantly in subsequent years of the study.  

Correlation of Serum and Urine Enzyme Activity in Patients with Acute Myocardial Infarction

1967 ◽  
Vol 13 (5) ◽  
pp. 359-370 ◽  
Author(s):  
Albert A Dietz ◽  
LaVerne K Hodges ◽  
Donald T Foxworthy
Keyword(s):  
Myocardial Infarction ◽  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Anticoagulation Therapy ◽  
Control Group ◽  
Average Value ◽  
Essentially Normal ◽  
Transmural Infarction ◽  
Urinary Acid

Abstract A correlation was made between the urinary excretion of GOT, GPT, LDH, HBD, and acid and alkaline phosphatase and their serum activity in 18 suspected cases of myocardial infarction. The diagnoses were made by a cardiologist without knowledge of the enzyme assays. The study included 2 cases of nontransmural infarction; 5 cases that had not sustained an infarction served as controls. Elevations of serum GOT, LDH, and HBD were found in 10 of 11 cases of transmural infarction, GPT and acid phosphatase in 5, and alkaline phosphatase in 7. Elevations in serum acid phosphatase were also found in the control group, and perhaps were related to the anticoagulation therapy. Urinary GOT and GPT activity was variable. Urinary LDH and HBD were elevated in 6 of the transmural infarction cases, usually when serum LDH and HBD activity was decreasing. Urinary acid phosphatase activity was essentially normal; but urinary alkaline phosphatase increased in 10 of the transmural infarction cases, and the average value remained high for more than 5 weeks. The only index that was elevated in all cases of acute transmural infarction was L-phenylalanine inhibition of urinary alkaline phosphatase activity.

Acid and alkaline phosphatases in the lymphomyeloid tissues of elasmobranch fish

1978 ◽  
Vol 58 (3) ◽  
pp. 727-730 ◽  
Author(s):  
Ragnar Fänge
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
High Activity ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Alkaline Phosphatases ◽  
Large Numbers ◽  
Alkaline Reaction ◽  
Elasmobranch Fish ◽  
Very High

Activities of phosphomonoesterases were measured at acid and at alkaline reaction (pH 4–5 or 9–65) in homogenates of elasmobranch tissues especially lymphomyeloid structures. The animals were dogfish (Scyliorhinus caniculd) and two species of ray (Raja brachyura, R. naevus). Acid phosphatase activity was high in the epigonal tissue, Leydig's organ, the spleen and the thymus. High activity was also found in the pancreas and the kidney, whereas skeletal and cardiac muscle showed low values. The activity of alkaline phosphatase was very high in the kidney and relatively low in other tissues. Ultrasonification of homogenates from the dogfish resulted in increase of acid phosphatase activity but had little effect on alkaline phosphatase activity. The high activity of acid phosphatase in lymphomyeloid tissue may be due to the presence of large numbers of various types of leucocytes.

Fluorometric Assay of Serum Acid or Alkaline Phosphatase, Either in Solution or on a Semisolid Surface

1975 ◽  
Vol 21 (12) ◽  
pp. 1791-1794 ◽  
Author(s):  
Bernd Rietz ◽  
George G Guilbault
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Clinical Laboratory ◽  
Serum Alkaline Phosphatase ◽  
Buffer Solution ◽  
Citrate Buffer ◽  
Enzymatic Action ◽  
Stable Substrate ◽  
Serum Acid Phosphatase

Abstract We describe enzymatic fluorometric methods for determining activities of serum alkaline phosphatase and of serum acid phosphatase in solution and on silicone rubber pads. 4-Methylumbelliferone phosphate is used as substrate, in either tris(hydroxymethyl)aminomethane or citrate buffer. In solution, the reaction is measured at 37 °C in a 3-ml Pyrex cuvette. Measurements on the pads are also made at 37 °C, after establishing a stable substrate film by lyophilizing all reagents on the surface of the pads. Only 20 to 30 µl of substrate solution, 50 µl of buffer solution, and 1 to 10 µl of blood are necessary, making a total volume of 51 to 60 µl for each assay. The rate of appearance of the fluorescent 4-methylumbelliferone liberated from 4-methylumbelliferone phosphate by the enzymatic action is measured and equated to enzyme activity. Calibration plots of the change in fluorescence per minute vs. enzyme activity for measurements in solution and on pads show a good proportionality in the range of 30.8 to 633 U/liter for alkaline phosphatase and in the range of 0.265 to 5.3 King— Armstrong units for acid phosphatase, indicating the usefulness of these methods in the clinical laboratory.

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