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.

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.

STEROID MEDIATED CHANGES OF LEUCOCYTE ALKALINE PHOSPHATASE ACTIVITY IN DOWN'S SYNDROME

PEDIATRICS ◽  
1966 ◽  
Vol 38 (6) ◽  
pp. 996-1002
Author(s):  
Ernest E. McCoy ◽  
Manuchair Ebadi ◽  
Jack England
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
X Chromosome ◽  
Alkaline Phosphatase Activity ◽  
Down's Syndrome ◽  
Down’S Syndrome ◽  
Chromosome 21 ◽  
G6pdh Activity ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Leucocyte Alkaline Phosphatase

A study of the increase of leucocyte alkaline phosphatase (LAP) activity following oral anhydroxyprogesterone or intramuscular prednisolone was carried out in a group of Down's syndrome subjects and paired controls. The increase in LAP activity was greater in the Down's syndrome patients at p < .025 with anhydroxyprogestrone and at p < .005 with prednisolone. Simultaneous assays were carried out in another group of patients for LAP and the X chromosome-linked enzyme glucose 6-phosphate dehydrogenase (G6PDH). The increase in LAP activity was greater in Down's syndrome but the increase in G6PDH activity was similar in the two groups. Several possible reasons for the greater increase in LAP activity following the steroids were discussed. The authors favor the view that the increase is related to greater rates of synthesis of the enzyme in Down's syndrome and to trisomy for chromosome 21.

Changes of elements in blood cells and enzyme activity in erythrocytes in down's syndrome (trisomy 21)

1998 ◽  
Vol 5 ◽  
pp. 80
Author(s):  
Erland Johansson ◽  
Tuomas Westermarck ◽  
Erkki Antila ◽  
Ulf Lindh ◽  
Päivi Nikkinen
Keyword(s):  
Enzyme Activity ◽  
Blood Cells ◽  
Trisomy 21 ◽  
Down's Syndrome ◽  
Down’S Syndrome

DYNAMICS OF ENZYME ACTIVITY AND SOME BLOOD ELEMENTS IN SHEEP PARASITOSIS

2021 ◽  
pp. 40-44
Author(s):  
A. N. Dudarchuk
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Gastrointestinal Tract ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Trointestinal Tract ◽  
Blood Elements

The article presents some studies on study of some aspects of pathogenesis in associative parasitosis of gas-trointestinal tract of sheep. As a result of the conducted studies, it was found that during spontaneous invasion of sheep by associations of parasites of gastrointestinal tract, following changes were established: a significant decrease in number of red blood cells by 1,77 times (P<0,001), hemoglobin-by 39,86 % (P<0,001), an increase in alanineaminotransferase and aspartateaminotransferase – by 1,59 times (P<0,01) and 1,42 times (P<0,001), alkaline phosphatase – by 1,32 times (P<0,001).

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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