scholarly journals Displacement of Acid Phosphatase and Alkaline Phosphatase Proteins in the Rat Kidney during a Dehydration Procedure. An Advantage of Ultrathin Frozen Sections for Detecting Precise Localization of an Enzyme Activity.

1995 ◽  
Vol 28 (2) ◽  
pp. 143-148
Author(s):  
Osamu Fukushima ◽  
Hideki Arakawa ◽  
Masaaki Kitada ◽  
Masakazu Miyamura ◽  
Takafumi Yatsu ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Rat Kidney ◽  
Precise Localization ◽  
Frozen Sections ◽  
Ultrathin Frozen Sections

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.

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.

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.

scholarly journals The distribution of some hydrolases in glomeruli and tubular fragments prepared from rat kidney by zonal centrifugation

1971 ◽  
Vol 122 (5) ◽  
pp. 641-645 ◽  
Author(s):  
D. G. Taylor ◽  
R. G. Price ◽  
D. Robinson
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Gel Electrophoresis ◽  
Leucine Aminopeptidase ◽  
Rat Kidney ◽  
Kidney Cortex ◽  
Starch Gel Electrophoresis ◽  
Multiple Forms ◽  
Rat Kidney Cortex ◽  
Starch Gel

1. A collagenase digest of rat kidney cortex was separated into four bands by zonal centrifugation. 2. Two of these bands were shown by light-microscopy to contain glomeruli and tubular fragments, which were free from each other and well separated from other renal material. 3. Protein, N-acetyl-β-glucosaminidase, 5′-nucleotidase, l-leucine β-naphthylamidase, leucine aminopeptidase, acid phosphatase and alkaline phosphatase were assayed across the gradient. 4. The greater proportion of these enzyme activities was recovered in the tubular fragments and acid phosphatase was the only enzyme detected in significant amounts in the glomeruli. 5. Tubular fragments and glomeruli were sedimented and multiple forms of β-naphthylamidase, N-acetyl-β-glucosaminidase, acid phosphatase and alkaline phosphatase were investigated by starch-gel electrophoresis.

PHOSPHATASE OF RABBIT POLYMORPHONUCLEAR LEUCOCYTES

1949 ◽  
Vol 27e (5) ◽  
pp. 290-307 ◽  
Author(s):  
D. M. Cram ◽  
R. J. Rossiter
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Bile Salts ◽  
Polymorphonuclear Leucocytes ◽  
Alkyl Sulphate ◽  
Low Concentrations ◽  
Activity Curve ◽  
Surface Active ◽  
Active Substances

Rabbit polymorphonuclear leucocytes contain an active phosphatase that readily hydrolyzes disodium phenyl phosphate. The pH activity curve of the enzyme was found to have two maxima, one in the region of pH 10 and the other in the region of pH 5. The alkaline phosphatase was much more active than the acid phosphatase. The concentration of alkaline phosphatase in rabbit white cells was approximately one thousand times that of the enzyme in the serum. Under the conditions of study, the alkaline phosphatase activity was proportional to the concentration of the enzyme. The effect of substrate concentration on the enzyme activity was studied and the Michaelis constant (Ks) determined. An excess of substrate inhibited the enzyme. The course of the reaction was linear with time for the first 60 min.; after 90 min. the activity fell off faster than would be expected if the reaction were of the first order.Magnesium and glycine, in low concentrations, caused an increase in the enzyme activity, whereas zinc, cyanide, borate, phosphate, bile salts, and glycine, in higher concentrations, were inhibitory. Fluoride had no demonstrable effect. Surface-active substances, such as saponin, bile salts, or alkyl sulphate, liberated the enzyme from the cells. Similar results were obtained when α-glycerophosphate or β-glycerophosphate was used as the substrate.The alkaline phosphatase can be considered to belong to Class AI of Folley and Kay (22) and the acid phosphatase to Class AII. The alkaline phosphatase can also be considered to be a Phosphatase II of Cloetens (9).

scholarly journals ULTRATHIN FROZEN SECTIONS

1967 ◽  
Vol 34 (3) ◽  
pp. 773-786 ◽  
Author(s):  
Elizabeth H. Leduc ◽  
W. Bernhard ◽  
S. J. Holt ◽  
J. P. Tranzer
Keyword(s):  
Enzyme Activity ◽  
Brush Border ◽  
Distal Tubule ◽  
Kidney Cortex ◽  
Mitochondrial Atpase ◽  
Frozen Sections ◽  
Enzyme Cytochemistry ◽  
Thin Sections ◽  
Ultrathin Frozen Sections ◽  
Structural Preservation

Endogenous enzyme activity can be readily and routinely demonstrated in ultrathin, frozen sections for electron microscopy. The procedure employed to obtain the best structural preservation as well as enzyme activity in thin sections involved fixation in glutaraldehyde, embedding in thiolated gelatin or pure gelatin, partial dehydration in glycerol, and sectioning in a cryostat at -35°C with a slightly modified Porter-Blum microtome on which the tissue is maintained at -70°C and the knife at -23°C. Kidney cortex was used as test tissue, but a few other organs were occasionally used. Thin sections were floated on the surface of several incubation media routinely employed for enzyme cytochemistry. Positive, specific reactions were obtained for alkaline phosphatase in kidney brush border, for adenosine triphosphatase in brush border and in basal membranes of distal tubules, for acid phosphatase and esterase in lysosomes, and for NADH diaphorase in mitochondria. Mitochondrial ATPase was sporadically evident only in the distal tubule of the kidney. Localizations of enzyme activity reported by other technical approaches were confirmed and in some cases somewhat improved.

Biochemical and histochemical studies of alkaline and acid phosphatases in a digenetic trematode,Pegosomum egretti

1986 ◽  
Vol 60 (4) ◽  
pp. 293-298 ◽  
Author(s):  
Indra Rajvanshi ◽  
K. L. Mali
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Raw Materials ◽  
Digenetic Trematode ◽  
Acid Phosphatases ◽  
Alkaline Phosphatases ◽  
Optimum Ph ◽  
Standard Techniques ◽  
Alkaline And Acid Phosphatases

ABSTRACTThe biochemistry and histochemistry ofPegosomum egrettihave been studied using standard techniques. Phosphatases were analysed colorimetrically; the optimum pH for acid phosphatase activity was 5·0 and for alkaline phosphatase was 10·0. The results were compared with those of other trematodes. Histochemical localization of acid and alkaline phosphatases revealed differences in enzyme activity in various tissues. These differences in the site and pattern of distribution of the two enzymes have been discussed in relation to transport of raw materials and the metabolism of the cell concerned.

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.

scholarly journals Lymphocyte and Granulocyte Enzyme Activity in Patients with Down’s Syndrome

Blood ◽  
1967 ◽  
Vol 30 (5) ◽  
pp. 669-673 ◽  
Author(s):  
HENRY L. NADLER ◽  
PATRICIA L. MONTELEONE ◽  
TOHRU INOUYE ◽  
DAVID YI-YUNG HSIA
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Blood Cells ◽  
Polymorphonuclear Leukocytes ◽  
White Blood Cells ◽  
Down's Syndrome ◽  
Down’S Syndrome ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Phosphatase Alkaline

Abstract Patients with trisomic Down’s syndrome were found to have significant increases of acid phosphatase, alkaline phosphatase, and glucose-6-phosphate dehydrogenase in both lymphocytes and polymorphonuclear leukocytes separated from white blood cells by the procedure of Rabinowitz. The alteration in enzyme activities appears not to be directly related to genes located on the chromosome causing Down’s syndrome.

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