Studies on phosphatase systems of cestodes I. Studies on Taenia pisiformis (Cysticercus and adult)

Parasitology ◽  
1957 ◽  
Vol 47 (1-2) ◽  
pp. 70-80 ◽  
Author(s):  
David A. Erasmus
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Life Cycle ◽  
Acid Phosphatase ◽  
Active Transport ◽  
Relative Magnitude ◽  
Alkaline Phosphatases ◽  
Biochemical Tests ◽  
Acid And Alkaline Phosphatase ◽  
Histochemical Tests

1. The phosphatases present in the adult and cysticercus stages of Taenia pisiformis have been investigated using histochemical and biochemical methods.2. Histochemical tests failed to demonstrate the sites of enzyme activity in the cysticercus.3. In the adult, the acid phosphatase is confined to the cuticle. Alkaline phosphatase occurs in the cuticle, subcuticular cells and the membranes bounding the ovary and vitelline tubules.4. The histochemical distribution is uneven along the length of the worm, both acid and alkaline phosphatase being predominant hi the region of ‘mature’ proglottides. The scolex was negative to both tests.5. Biochemical tests have demonstrated distinct acid and alkaline phosphatases in the cysticercus and adult stages. In the cysticercus the acid enzyme is predominant and in the adult it is the alkaline, implying a change in relative magnitude during the completion of the life cycle.6. pH-activity curves have been obtained for the enzymes of both stages.7. The results are discussed in relation to recent findings in the field of cestode enzymology, and it is suggested that these phosphatases may be associated with active transport of materials across the cuticle and ovarian and vitelline membranes.

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.

Studies on host specificity in Paragonimus westermani: II. Histochemical and cytochemical characterization of metacercariae and worms from rats and dogs

1989 ◽  
Vol 63 (4) ◽  
pp. 315-327 ◽  
Author(s):  
Takahiro Fujino ◽  
Koichi Fukuda ◽  
Fusanori Hamajima ◽  
Yoichi Ishii
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Atpase Activity ◽  
Phosphatase Activity ◽  
Metabolic Activity ◽  
Acid And Alkaline Phosphatase ◽  
Excretory Bladder ◽  
Histochemical Tests ◽  
Parenchymal Cells

ABSTRACTHistochemical tests were done on newly excysted metacercariae and worms recovered from an abnormal host (rat) and the definitive host (dog) for some oxidoreductases, phosphatases and glycosidases. The results demonstrate that rat worms have enzymatic distribution and intensities more similar to those of metacercariae than to adult worms from dogs. Ultracytochemical examination of acid and alkaline phosphatase and Mg-ATPase activity was also carried out. Acid phosphatase activity occurred exceptionally in the excretory bladder and caeca of dog worms. No activity was observed in rat worms except for lysosomal granules in the tegument. Alkaline phosphatase activity was exhibited in the excretory bladder in both dog and rat worms. Mg-ATPase activity occurred in the tegument and parenchymal cells in dog worms and in the excretory bladder in rat worms. In metacercariae, little or no reaction for these enzymes was present except for Mg-ATPase activity on the excretory ducts. These observations, together with the histochemical results, indicate that metabolic activity in rat worms is higher than in metacercariae although it is strongly reduced compared with dog worms.

Studies on phosphatase systems of cestodes II. Studies on Cysticercus tenuicollis and Moniezia expansa (adult)

Parasitology ◽  
1957 ◽  
Vol 47 (1-2) ◽  
pp. 81-91 ◽  
Author(s):  
David A. Erasmus
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
The Body ◽  
Biochemical Tests ◽  
Cysticercus Tenuicollis ◽  
Acid And Alkaline Phosphatase ◽  
Incubation Experiments ◽  
Biochemical Studies ◽  
Moniezia Expansa

1. Histochemical and biochemical studies have demonstrated the presence and distribution of phosphatases in Cysticercus tenuicollis and adult Moniezia expansa.2. Biochemical tests have differentiated the following types of optimum phosphatase activity: Cysticercus tenuicollis, acid phosphatase, pH 5·0 (approx.); alkaline phosphatase, pH 10·0 (approx.); Moniezia expansa, acid plaosphatase, pH 5·5 (approx.); alkaline phosphatase, pH 7·0–8·0 and pH 10·0–11·0.3. Attempts to locate the enzymes by normal histochemical methods were unsuccessful in the case of Cysticercus tenuicollis. In adult Moniezia, acid and alkaline phosphatase (both types) occurred in the cuticle. Alkaline phosphatase (pH 10·0–11·0) only was present in the tunicae enclosing the ovary, vitelline gland and testes. This enzyme was also the only one present in the interproglottidal glands, in the wall of the developing uterus and in the subcuticular cells.4. Tests for all types of phosphatase activity showed that cuticular activity in Moniezia originated in the walls of an extensive branched system of channels. This system was demonstrable in the cuticle of fixed and unfixed material.5. Incubation experiments with entire living Moniezia showed that substrates external to the body were capable of being broken down. Similar tests with Cysticercus tenuicollis showed that at least some of the alkaline phosphatase activity recorded by the biochemical tests was located in the cuticle.

Effects of Kanwa on Rat Gastrointestinal Phosphatases

2010 ◽  
Vol 3 (3) ◽  
pp. 1147-1152
Author(s):  
Jacob Bamaiyi ◽  
Omajali ◽  
Sanni Momoh
Keyword(s):  
Alkaline Phosphatase ◽  
Small Intestine ◽  
Acid Phosphatase ◽  
Sodium Carbonate ◽  
Elevated Level ◽  
Food Additive ◽  
Alkaline Phosphatases ◽  
Acid And Alkaline Phosphatases ◽  
Diagnostic Indices ◽  
High Level

This study investigates the effects of kanwa on rat gastrointestinal phosphatases. The rats were administered 7% w/v concentration of  trona (Kanwa) orally for a period of two weeks in order to investigate how this compound is being used as food additive in some homes in Nigeria. The Kanwa used in this study was the handpicked variety obtained from sellers from Anyigba market in eastern part of Kogi State, Nigeria. Kanwa, a hydrated sodium carbonate (Na2CO3NaHCO3.2H2O) was obtained as a dried lake salt. Acid phosphatase has the ability to dephosphorylate molecules containing phosphate group. The decreased and elevated level in serum or plasma acid and alkaline phosphatases serves as diagnostic indices for various diseases. Results showed that there was increase and decrease of acid phosphatase (ACP) activities in both the stomach and small intestine. The activities of alkaline phosphatase (ALP) fluctuated in the small intestine. However, in the stomach, an increase activity of ALP was noticed throughout the period of ‘Kanwa’ administration. We concluded that although the level of ‘Kanwa’ consumed in most homes may not be toxic if not taken continuously or repeatedly. Thus, continuous consumption should be discouraged as accumulation of high level of ‘Kanwa’ may cause damages or injuries to the various organs/tissues and may disrupt normal body function.

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.

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.

scholarly journals HISTOCHEMICAL DEMONSTRATION OF ACID PHOSPHATASE ACTIVITY IN OSTEOCLASTS

1959 ◽  
Vol 7 (1) ◽  
pp. 39-41 ◽  
Author(s):  
M. S. BURSTONE
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Comparative Studies ◽  
Acid Phosphatase Activity ◽  
Azo Dye ◽  
Histochemical Demonstration ◽  
Accurate Localization ◽  
Acid And Alkaline Phosphatase ◽  
Cold Acetone

High acid phosphatase activity was observed in osteoclasts of several species using a reproducible azo-dye technique. High activity of two distinct enzymes, acid and alkaline phosphatase, are associated with osteoclasts and osteoblasts respectivey. Althouth frozen-dried tissues are recommended for definitive studies, the enzyme techniques used give satisfactory results with cold acetone-fixed tissues. The most accurate localization of acid phosphatase in osteoclasts in controlled comparative studies is obtained with double-embedded frozen-dried undecalcified tissues in conjunction with naphthol AS-phosphates.

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