The ultrastructural localization of acid phosphatase, alkaline phosphatase and adenosine triphosphatase in induced goitres of Xenopus laevis Daudin tadpoles

1967 ◽  
Vol 10 (1) ◽  
pp. 33-43 ◽  
Author(s):  
R. Coleman ◽  
P. J. Evennett ◽  
J. M. Dodd
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Xenopus Laevis ◽  
Adenosine Triphosphatase ◽  
Ultrastructural Localization ◽  
Phosphatase Alkaline

Histochemical localization of phosphomonoesterases in Avhellina lahorea Woodland, 1927 (Cestoda: Anoplocephalida)

1984 ◽  
Vol 58 (2) ◽  
pp. 169-173 ◽  
Author(s):  
Rashid Farooq ◽  
H.U. Farooqi
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Adenosine Triphosphatase ◽  
Intestinal Parasite ◽  
Histochemical Localization ◽  
Sheep And Goats ◽  
Almost All ◽  
Phosphatase Alkaline

AbstractNon-specific and specific phosphatases have been histochemically localized in the tissues of Avitellina lahorea, an intestinal parasite of sheep and goats. Large quantities of acid phosphatase, alkaline phosphatase and adenosine triphosphatase were observed in almost all organs except the parenchyma where there were moderate amounts of acid phosphatase and no alkaline phosphatase; the reproductive ducts contained moderate amounts of alkaline phosphatase. 5-nucleotidase was observed only in the uterus, egg pouches and eggs and glucose-6-phosphatase activity was restricted to the tegument. The probable functions of these moieties at different sites are discussed.

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.

Histochemical studies on Raillietina (Raillietina) johri (Cestoda: Davaineidae). I. Nonspecific and specific phosphatases

1979 ◽  
Vol 53 (1) ◽  
pp. 45-49 ◽  
Author(s):  
T. K. Roy
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Atpase Activity ◽  
Functional Significance ◽  
Adenosine Triphosphatase ◽  
Vas Deferens ◽  
Gland Cells ◽  
Vitelline Gland ◽  
Receptaculum Seminis ◽  
Almost All

ABSTRACTCertain phosphatases have been localized by histochemical techniques in various tissues of a pigeon cestode, Raillietina (Raillietina) johri. Acid phosphatase (AcPase), alkaline phosphatase (AlPase) and adenosine triphosphatase (ATPase) were present in almost all structures: tegument; subtegumental muscles; subtegumental cells; excretory canal; tsetes; sperm ductules; vas deferens; cirrus sac; cirrus; ovary; receptaculum seminis; vagina; vitelline gland cells; oocytes; uterus; embryonated eggs. AlPase was absent in parenchyma, spermatocytes, spermatids and spermatozoa. AlPase activity was more intense in the tegument of mature gravid proglottides. AcPase and ATPase were visualized in various stages of spermatogenesis of the parasite. ATPase activity was also observed in chromosomes. 5'-nucleotidase (AMPase) activity was restricted to embryonated eggs only. Functional significance of these phosphatases is discussed.

A Histological and Histochemical Study of the Brown and Yellow Adipose Tissue of the Bat, Hipposideros speoris

1959 ◽  
Vol s3-100 (51) ◽  
pp. 369-375
Author(s):  
J. C. GEORGE ◽  
J. EAPEN
Keyword(s):  
Alkaline Phosphatase ◽  
Adipose Tissue ◽  
Acid Phosphatase ◽  
Adenosine Triphosphatase ◽  
Succinic Dehydrogenase ◽  
Lactic Dehydrogenase ◽  
Histological Structure ◽  
Brown Adipose ◽  
Aldehydes And Ketones ◽  
Sulphydryl Groups

A study of the histology and histochemical reactions for lipase, alkaline phosphatase, acid phosphatase, adenosine triphosphatase, succinic dehydrogenase, lactic dehydrogenase, phospholipids, cholesterol, sulphydryl groups, and water-insoluble aldehydes and ketones in the brown and yellow adipose tissue of the bat (Hipposideros speoris) revealed that the two types of adipose tissue differ in histological structure as well as physiological activity. The histological structure of the two types of adipose tissue was found to be different, resembling that of the two corresponding types of the rat. The brown adipose tissue showed a higher concentration of succinic dehydrogenase, lactic dehydrogenase, phospholipids, cholesterol, and sulphydryl groups. No detectable difference between brown and yellow adipose tissue was, however, found with respect to lipase, alkaline phosphatase, acid phosphatase, adenosine triphosphatase, and water-insoluble aldehydes and ketones.

scholarly journals CYTOCHEMISTRY AND ELECTRON MICROSCOPY

1963 ◽  
Vol 17 (1) ◽  
pp. 19-58 ◽  
Author(s):  
David D. Sabatini ◽  
Klaus Bensch ◽  
Russell J. Barrnett
Keyword(s):  
Electron Microscopy ◽  
Alkaline Phosphatase ◽  
Fine Structure ◽  
Acid Phosphatase ◽  
Adenosine Triphosphatase ◽  
Osmium Tetroxide ◽  
Enzyme Histochemistry ◽  
Succinic Dehydrogenase ◽  
Optimal Conditions ◽  
Fixation Procedure

The aldehydes introduced in this paper and the more appropriate concentrations for their general use as fixatives are: 4 to 6.5 per cent glutaraldehyde, 4 per cent glyoxal, 12.5 per cent hydroxyadipaldehyde, 10 per cent crotonaldehyde, 5 per cent pyruvic aldehyde, 10 per cent acetaldehyde, and 5 per cent methacrolein. These were prepared as cacodylate- or phosphate-buffered solutions (0.1 to 0.2 M, pH 6.5 to 7.6) that, with the exception of glutaraldehyde, contained sucrose (0.22 to 0.55 M). After fixation of from 0.5 hour to 24 hours, the blocks were stored in cold (4°C) buffer (0.1 M) plus sucrose (0.22 M). This material was used for enzyme histochemistry, for electron microscopy (both with and without a second fixation with 1 or 2 per cent osmium tetroxide) after Epon embedding, and for the combination of the two techniques. After fixation in aldehyde, membranous differentiations of the cell were not apparent and the nuclear structure differed from that commonly observed with osmium tetroxide. A postfixation in osmium tetroxide, even after long periods of storage, developed an image that—notable in the case of glutaraldehyde—was largely indistinguishable from that of tissues fixed under optimal conditions with osmium tetroxide alone. Aliesterase, acetylcholinesterase, alkaline phosphatase, acid phosphatase, 5-nucleotidase, adenosine triphosphatase, and DPNH and TPNH diaphorase activities were demonstrable histochemically after most of the fixatives. Cytochrome oxidase, succinic dehydrogenase, and glucose-6-phosphatase were retained after hydroxyaldipaldehyde and, to a lesser extent, after glyoxal fixation. The final product of the activity of several of the above-mentioned enzymes was localized in relation to the fine structure. For this purpose the double fixation procedure was used, selecting in each case the appropriate aldehyde.

scholarly journals Cytochemical localization of certain hydrolytic enzymes at various stages of development of Achlya flagellata mycelium

2015 ◽  
Vol 41 (2) ◽  
pp. 265-282 ◽  
Author(s):  
I. Palczewska ◽  
G. Jagodzka
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Azo Dyes ◽  
Acid Phosphatase Activity ◽  
Hydrolytic Enzymes ◽  
Cytochemical Localization ◽  
Cytoplasmic Granules ◽  
End Products ◽  
E 600 ◽  
Phosphatase Alkaline

The standard coupling azo dyes techniques were used to reveal the activities of acid phosphatase, alkaline phosphatase, esterase and β-galactoidase in the vegetative and reproductive cycle of <i>Achlya flagellata</i>. The end-products of the enzymic reactions, with the exception of E 600 sentisive esterese, which is localized in cytoplasm, occured in cytoplasmic granules. These granules are expected to be spherosomes. Acid phosphatase activity is high in differentiating sporangia, in antheridial hyphae and in degenerating oospheres where hydrolytic processes occur. β-galactosidase is the least active enzyme in the mycelium of <i>Achlya</i>.

scholarly journals Enzyme histochemistry of developing rat oral mucosa.

1981 ◽  
Vol 29 (1) ◽  
pp. 57-64 ◽  
Author(s):  
S Sjögren ◽  
L Hammarström ◽  
A Larsson
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Lactate Dehydrogenase ◽  
Succinate Dehydrogenase ◽  
Oral Mucosa ◽  
Adenosine Triphosphatase ◽  
Enzyme Histochemistry ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Developing Rat

The oral mucosa of developing and mature rats was analyzed histochemically for regional enzyme differences. The following enzymes were studied: nonspecific alkaline phosphatase (alkpase), acid phosphatase (acidpase), 5'-nucleotidase (AMPase), adenosine triphosphatase (ATPase), succinate dehydrogenase (SDH), lactate dehydrogenase (LDH), and glucose-6-phosphate dehydrogenase (G-6-pDH). All enzymes were active in the oral mucosa, but regional as well as tissue variations were observed. Epithelium in all regions showed acidpase staining. Oxidoreductases were found in all regions with variations within the epithelium. The epithelium of specific regions stained for alkpase and AMPase, while adjacent epithelium did not. We suggest that the alkpase and AMPase activities are associated with specific functions of the epithelium in these regions.

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