scholarly journals HISTOCHEMICAL DEMONSTRATION OF CHANGES IN THE ACTIVITY OF ALKALINE AND ACID PHOSPHATASES IN THE ADRENAL OF A MIGRATORY STARLING

1964 ◽  
Vol 12 (10) ◽  
pp. 772-776 ◽  
Author(s):  
D. V. NAIK ◽  
J. C. GEORGE
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Adrenal Cortex ◽  
Adrenocorticotropic Hormone ◽  
Acid Metabolism ◽  
Histochemical Demonstration ◽  
Nucleic Acid Metabolism ◽  
Acid Phosphatases ◽  
Very High ◽  
Alkaline And Acid Phosphatases

The activity of alkaline and acid Phosphatases was studied in adrenal cortex and medulla at the beginning and the end of the period of preparation for migration in the migratory starling, Sturnus roseus. Alkaline phosphatase in cortex and acid phosphatase in medulla showed very high increases as migration approached. The increase in alkaline phosphatase activity is correlated with increase in adrenocorticotropic hormone, ribonucleic acid, corticoids and fat in adrenal cortex, and the increase in acid phosphatase in adrenal medulla with increase in adrenalin and nor-adrenalin production. The increase in acid phosphatase in the nuclei of the cortical and medullary cells is correlated with increased nucleic acid metabolism.

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.

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.

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.

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.

MUCINOGENESIS AND ENZYMORPHOLOGY OF RAT VAGINA; PHOSPHORYLASE, β-GLUCURONIDASE, DPNH-DIAPHORASE AND PHOSPHATASES

1962 ◽  
Vol 39 (3) ◽  
pp. 395-406 ◽  
Author(s):  
Tadao Takeuchi ◽  
Masando Hayashi ◽  
William H. Fishman
Keyword(s):  
Alkaline Phosphatase ◽  
Subcutaneous Injection ◽  
Ovariectomized Rats ◽  
Acid Phosphatases ◽  
Hormonal Stimulation ◽  
Close Relationship ◽  
Physiologic Function ◽  
Intracellular Metabolism ◽  
Epithelial Layers ◽  
Alkaline And Acid Phosphatases

ABSTRACT Vaginal epithelium of ovariectomized rats following the subcutaneous injection of oestrogenic hormone was analyzed by enzymorphology and particular attention was given to mucin formation. Localization and intensity of enzymes examined in this study such as amylophosphorylase, amylo-1,4→ 1,6-transglucosidase, alkaline and acid phosphatases, 5-nucleotidase, esterase, DPNH-diaphorase, and β-glucuronidase varied depending on the stage of hormonal stimulation. Mucified cells contained the various enzymes examined, being especially rich in phosphorylase, alkaline phosphatase, 5-nucleotidase, β-glucuronidase and DPNH-diaphorase. These seemed to be related to the intracellular metabolism in the mucinogenous cells of epithelial layers. One of these, amylophosphorylase was demonstrated only in mucified cells within whole epithelial layers in mucified stage, and a close relationship between it and mucin formation was observed. The location of amylo-1,4→ 1,6-transglucosidase resembled the phosphorylase finding and suggests a similar physiologic function.

scholarly journals A Study on Evaluation of Alkaline and Acid Phosphatase Isozymes During Different Developmental Stages of New Breeding Lines and Races of Bombyx mori L

2021 ◽  
pp. 293-299
Author(s):  
Manjula A. C. ◽  
Keshamma E
Keyword(s):  
Acid Phosphatase ◽  
Bombyx Mori ◽  
Developmental Stages ◽  
Colorimetric Determination ◽  
Acid Phosphatases ◽  
Breeding Lines ◽  
Bombyx Mori L ◽  
Alkaline And Acid Phosphatase ◽  
Post Coupling ◽  
Alkaline And Acid Phosphatases

It is interesting to note that different silkworm races reared in laboratory offer an important testing ground for the application of biochemical methods to taxonomic problems. Moreover, there is scarcity of knowledge on enzyme studies in new breeding lines and races of silkworm specially Bombyx mori L. Therefore, we designed the present study with the main goal to evaluate the activities of alkaline and acid phosphatases quantitatively during different developmental stages of new breeding lines and races viz. Kalimpong-A (KA), B18, Pure Mysore (PM), evolved R1 and R2 of Bombyx mori L. Quantitative estimations of in alkaline and acid phosphatases were expressed in terms of enzyme activity. Alkaline and acid phosphatase activities during the different developmental stages of KA, NB18, PM, evolved R1 & R2 races were determined using Sodium-1 naphthahyl phosphate as a substrate following the dye-coupling method. The assay mixture included 2 ml of substrate and 0.2 ml of enzyme extract and incubation was made for 30 minutes at 25°c. The reaction was stopped by adding 2 ml of post coupling solution (5 parts of 4% sodium dodecyl sulphate and 2 parts of 0.2% Fast red TR salt) and colorimetric determination were made at 540 nm. Results illustrated that the activity of phosphatases was found to be different and high activity was found in the larval stage, which is feeding stage followed by pupae.

Ultracytochemical Localization of Aryl Sulfatase, Esterase, and Acid and Alkaline Phosphatases with 4-Nitrocatechol Substrates and Tetrazolium Salts

1974 ◽  
Vol 32 ◽  
pp. 226-227
Author(s):  
W. Allen Shannon ◽  
Yoshinobu Hoshino ◽  
Hannah L. Wasserkrug ◽  
Arnold M. Seligman
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Adrenal Cortex ◽  
Rat Kidney ◽  
Kidney Cortex ◽  
Alkaline Phosphatases ◽  
Cytochemical Localization ◽  
Rat Kidney Cortex ◽  
Aryl Sulfatase ◽  
Tetrazolium Salts

The ultra cytochemical localization of various hydrolases, i. e, aryl sulfatase(ArS), esterase (Est), acid phosphatase(AcP) and alkaline phosphatase (A1P) is demonstrated in rat kidney cortex with newly developed 4-nitrocatechol substrates (2-hydroxy-5-nitrophenyl compounds) (Fig. 1) and tetrazolium salts, Nitro-BT, BSPT, and BPPT. ArS was also investigated in adrenal cortex.

A Comparison of the Histochemical Enzyme Pattern in Normal and Varicose Veins

1987 ◽  
Vol 2 (3) ◽  
pp. 135-158 ◽  
Author(s):  
Bernhardt Haardt
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Lysosomal Enzymes ◽  
Adenosine Triphosphatase ◽  
Varicose Veins ◽  
Histochemical Demonstration ◽  
Saphenous Veins ◽  
The Media ◽  
Enzyme Pattern

In order to study enzyme activity in the walls of healthy and diseased veins, sections were taken from the stripped varicose long saphenous veins of eight patients. These were subjected to histochemical enzyme investigations. These methods were used to determine levels and localization of lactate dehydrogenase, alkaline phosphatase, adenosine triphosphatase and the lysosomal enzymes, β-glucuronidase, non-specific esterases and acid phosphatase. The method and our findings are described. The results of these histochemical investigations demonstrate an increase in lysosomal enzyme activity in the walls of varicose veins as compared to that of normal veins. This increase is greater in the media than in the intima. Enzymes responsible for energy metabolism demonstrated contradictory behaviour, with decline in the activity of such enzymes in the walls of varicose veins. This decline in enzyme activity was more marked in the intima than in the media and was especially noticeable in the histochemical demonstration of Ca++-adenosine triphosphatase.

The Demonstration of Human Prostatic Acid Phosphatase (Pap) With Phosphorylcholine

1976 ◽  
Vol 34 ◽  
pp. 88-89
Author(s):  
José A. Serrano ◽  
Hannah L. Wasserkrug ◽  
Anna A. Serrano ◽  
Arnold M. Seligman
Keyword(s):  
Acid Phosphatase ◽  
Prostate Gland ◽  
Prostatic Acid Phosphatase ◽  
Human Prostate ◽  
Rat Tissues ◽  
Specific Substrate ◽  
Acid Phosphatases ◽  
Lysosomal Acid ◽  
Cacodylate Buffer

As previously reported (1, 2) phosphorylcholine (PC) is a specific substrate for prostatatic acid phosphatase (PAP) as opposed to other acid phosphatases, e.g., lysosomal acid phosphatase. The specificity of PC for PAP is due to the pentavalent nitrogen in PC, a feature that renders PC resistant to hydrolysis by all other acid phosphatases. Detailed comparative cytochemical results in rat tissues are in press. This report deals with ultracytochemical results applying the method to normal and pathological human prostate gland.Fresh human prostate was obtained from 7 patients having transurethral resections or radical prostatectomies. The tissue was fixed in 3% glutaraldehyde- 0.1 M cacodylate buffer (pH 7.4) for 15 min, sectioned at 50 μm on a Sorvall TC-2 tissue sectioner, refixed for a total of 2 hr, and rinsed overnight in 0.1 M cacodylate buffer (pH 7.4)-7.5% sucrose.

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