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.

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.

scholarly journals ACID AND ALKALINE PHOSPHATASE IN WHITE CELLS DATA FOR THE LYMPHOCYTE AND THE POLYMORPHONUCLEAR LEUKOCYTE OF MAN AND THE RABBIT

Blood ◽  
1950 ◽  
Vol 5 (3) ◽  
pp. 267-277 ◽  
Author(s):  
W. F. HAIGHT ◽  
R. J. ROSSITER
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Statistical Analysis ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Human Cell ◽  
Human Lymphocyte ◽  
Polymorphonuclear Leukocyte ◽  
Cell Suspensions ◽  
Acid And Alkaline Phosphatase

Abstract 1. The acid and alkaline phosphatase activity has been determined on a series of suspensions of white cells obtained from both man and the rabbit by several different methods. 2. A statistical analysis of the results shows that for both species the alkaline phosphatase of white cell suspensions is confined chiefly to the polymorphonuclear leukocyte and the acid phosphatase is chiefly in the lymphocyte, although the polymonphonuclear leukocyte contains lesser concentrations of this enzyme also. 3. Although this qualitative distribution was the same for both species studied, quantitatively the rabbit differed from man. The activity of the alkaline phosphatase of the rabbit polymorphonuclear leukocyte was eight times that of the corresponding human cell, while the activity of the acid phosphatase of the human lymphocyte was more than twice that of rabbit lymphocyte.

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.

scholarly journals DISTRIBUTION OF ACID AND ALKALINE PHOSPHATASE ACTIVITY IN UNDEMINERALIZED SECTIONS OF THE RAT TIBIAL DIAPHYSIS

1969 ◽  
Vol 17 (12) ◽  
pp. 799-806 ◽  
Author(s):  
JON E. WERGEDAL ◽  
DAVID J. BAYLINK
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Strong Activity ◽  
Acid And Alkaline Phosphatase ◽  
Periosteal Cell ◽  
Rat Tibia ◽  
Tetracycline Labeling

The distribution of acid and alkaline phosphatase activity in the rat tibia has been studied in transverse sections sawed from fresh undemineralized diaphyses. The endosteal resorbing surfaces had the highest acid phosphatase activity as demonstrated with 50 mM α-naphthol phosphate as the substrate. Strong activity was present not only in osteoclasts and adjacent osteocytes but extracellularly lining Howship's lacunae. In areas of bone formation, moderate acid phosphatase activity was present in osteoblasts and young osteocytes. In addition, a zone of activity was found at the mineralizing front where mineralization is initiated. This active zone ( a) was separated from the active periosteal cell layer by a zone of inactive osteoid and ( b) in formol-calcium-fixed demineralized sections extended into young bone. The identity of the mineralizing front was confirmed by tetracycline labeling. The activity at the mineralizing front had the properties of an enzyme. Alkaline phosphatase activity demonstrated with naphthol ASTR phosphate was largely associated with the osteoblasts and other mesenchymal cells at forming surfaces.

Effect of Alkaline and Acid Phosphatases on Clotting:

1966 ◽  
Vol 15 (03/04) ◽  
pp. 365-380 ◽  
Author(s):  
P. G Iatridis ◽  
J. H Ferguson
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Inhibitory Effect ◽  
Factor Ix ◽  
Acid Phosphatases ◽  
Acid And Alkaline Phosphatase ◽  
Direct Inhibitory Effect ◽  
Alkaline And Acid Phosphatases

SummaryAlkaline phosphatase is found to enhance the activation of factor IX by SF. The correlation of the distribution of alkaline phosphatase in electrophoretic fractions with the clotting tests suggest that the “beta” fraction contains the responsible factor for the acceleratory effect of alkaline phosphatase on clotting.Acid phosphatase, while not exerting a direct inhibitory effect on SF, does enhance the plasmatic anti-SF activity. The “beta” and “F-gamma” fractions seem to contain the responsible factor of acid phosphatase for the plasmatic anti-SF enhancement.SF preparation has no acid or alkaline phosphatase activity.A tentative schema is proposed to explain the effects of acid and alkaline phosphatase on clotting.

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.

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.

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