ENZYMORPHOLOGIC OBSERVATIONS IN THE UTERUS AND VAGINA OF CASTRATE RATS RECEIVING OVARIAN HORMONES

1961 ◽  
Vol 38 (1) ◽  
pp. 107-120 ◽  
Author(s):  
Masando Hayashi ◽  
William H. Fishman
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Ovarian Hormones ◽  
The Other ◽  
Histochemical Localization ◽  
Phosphatase Activities ◽  
Other Hand ◽  
Small Doses ◽  
Phosphatase Alkaline

ABSTRACT The early changes in the histochemical localization of β-glucuronidase, α-naphthy esterase, acid phosphatase, alkaline phosphatase and reduced diphosphopyridine nucleotide diaphorase (DPNH-diaphorase) were investigated in the uterus and the vagina of castrate rats following treatment with 17β-oestradiol alone, and with progesterone in animals previously primed with oestradiol. Marked alterations in the intensity and location of β-glucuronidase, esterase and alkaline phosphatase occur in the vagina only two hours after the injection of oestrogen. On the other hand, the change in DPNH-diaphorase or acid phosphatase is much slower in making its appearance. Progesterone accelerates these effects in animals previously primed with small doses of oestrogen. Among the changes observed, the most characteristic are the ones occurring in the β-glucuronidase and alkaline phosphatase activities of the vagina.

scholarly journals BETA GLUCURONIDASE-RICH CYTOPLASMIC PARTICLES IN ANDROGEN-STIMULATED MOUSE KIDNEY

1963 ◽  
Vol 16 (2) ◽  
pp. 253-258 ◽  
Author(s):  
Andrew G. Plaut ◽  
William H. Fishman
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Specific Activity ◽  
Mouse Kidney ◽  
The Other ◽  
Mouse Testis ◽  
Glucuronidase Activity ◽  
Other Hand ◽  
Fraction I ◽  
Gonadotropic Hormones

Androgens produced by stimulating mouse testis with gonadotropic hormones cause a rise in renal ß-glucuronidase but not an increase in acid or alkaline phosphatase. All subcellular components increase in ß-glucuronidase activity, with a relatively greater increment in particulate enzyme as compared with that free in the cytoplasm (non-sedimentable). A small percentage of recovered ß-glucuronidase, acid phosphatase, and alkaline phosphatase is found in material which rises to the surface during centrifugation in sucrose media (fraction I). The specific activity of ß-glucuronidase and acid phosphatase in this fraction is normally quite high with respect to the homogenate, while that of alkaline phosphatase is not. On the other hand, the fraction I material from androgen-stimulated mice exhibits a further increase in specific activity with respect to ß-glucuronidase and not acid phosphatase. It thus appears that there is an independence in the behavior of individual enzymes in response to physiologic stimuli in spite of obvious morphologic proximity.

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.

scholarly journals Clasmatosis in Sea Star Immune Responses Observed in T.E.M Invertebrate Antibody. Biosynthesis in Anti-Hrp Responses And In Anti-Alkaline Phosphatase Responses

2020 ◽  
Vol 1 (4) ◽  
Author(s):  
Michel Leclerc
Keyword(s):  
Alkaline Phosphatase ◽  
Golgi Apparatus ◽  
Immune Responses ◽  
The Other ◽  
Sea Star ◽  
Other Hand

Anti-HRP (Horse-radish peroxydase) and Anti-Alkalin phosphatase immunocytochemical responses occur in Asterina gibbosa (Asterid Echinodermata) after immunizations to HRP and, on the other hand to Alkalin phosphatase enzymes. Classical TEM observations from ergastoplasmic labelling to Golgi apparatus one were done : they shown also “clasmatosis phenomenon” and recall , in a general way invertebrate antibody biosynthesis.

COMPOSITION OF EPIPHYSEAL CARTILAGE: III. DIFFERENCES IN ENZYMATIC ACTIVITIES OF EPIPHYSEAL AND ARTICULAR CARTILAGES OF RACHITIC CHICKS

1962 ◽  
Vol 40 (4) ◽  
pp. 419-423 ◽  
Author(s):  
J. D. Cipera ◽  
J. S. Willmer
Keyword(s):  
Alkaline Phosphatase ◽  
Articular Cartilage ◽  
Comparative Study ◽  
Adenosine Triphosphatase ◽  
Enzymatic Activities ◽  
The Other ◽  
Epiphyseal Cartilage ◽  
Other Hand ◽  
Articular Cartilages

From a comparative study of enzymatic activities in epiphyseal and articular cartilages of 3-week-old rachitic chicks it appears that the activities of pyrophosphatase and adenosine triphosphatase are approximately four times higher in epiphyseal than in articular cartilage. The greater activity of epiphyseal cartilage is even more pronounced in the cases of alkaline phosphatase and hexosamine synthetase. Phosphorylase, on the other hand, is more active in articular cartilage. The significance of these observations is discussed.

Lysosomal Enzyme Activities in Platelets of Normal Individuals and of Patients with Gaucher’s Disease

1974 ◽  
Vol 32 (02/03) ◽  
pp. 665-669 ◽  
Author(s):  
S Yatziv ◽  
M White ◽  
A Eldor
Keyword(s):  
Acid Phosphatase ◽  
Lysosomal Enzyme ◽  
Enzyme Activities ◽  
The Other ◽  
Gaucher's Disease ◽  
Gaucher’S Disease ◽  
Other Hand ◽  
Normal Individuals ◽  
Specific Activities ◽  
Normal Controls

SummaryFive platelet lysosomal enzyme activities were estimated in 22 normal individuals and in 5 patients with Gaucher’s disease: ß-D-galactosidase, N-Acetyl-ß-D-glucosa-minidase, N-Acetyl-ß-D-galactosaminidase acid-phosphatase, and ß-D-glucuronidase.In the 5 patients with Gaucher’s disease the specific activities for the first four of these enzymes were significantly higher than in normal individuals. The activity of acid-phosphatase, on the other hand, was lower in G. d. than in normals. The release of the 5 lysosomal enzymes from platelets upon incubation with thrombin was also examined in the same two groups. The only lysosomal enzyme that was not released from normal platelets was acid-phosphatase. In Gaucher’s patients, on the other hand, acid-phosphatase was invariably released from platelets when incubated with thrombin. The release of the other four enzymes from platelets of Gaucher patients was similar to that of normal controls.

Soil enzyme activities following paper sludge addition in a winter cabbage-sweet corn rotation

2000 ◽  
Vol 80 (1) ◽  
pp. 91-97 ◽  
Author(s):  
B. Gagnon ◽  
R. Lalande ◽  
R. R. Simard ◽  
M. Roy
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Sweet Corn ◽  
Soil Enzyme ◽  
Phosphatase Activities ◽  
Arylsulfatase Activity ◽  
Papermill Sludge ◽  
Soil Acid Phosphatase

Combined primary and secondary papermill sludge (PS) is a good source of C and other nutrients for soils devoted to intensive horticultural production. A field study was conducted to evaluate the effect of PS, spring-applied alone or in combination with ammonium nitrate (AN), on the enzymatic activity of a Bedford clay (Humic Gleysol) in the province of Québec, Canada. The experiment was started in 1996 with winter cabbage (Brassica oleracea var. capitata L.) and continued in 1997 and 1998 on the same plots with sweet corn (Zea mays L.). The PS was applied at 0 (control), 8, 16, 32 and 65 Mg ha−1 in 1996 and at 44% of these rates in 1997. No sludge was applied in 1998. Additional treatments consisted of AN applied yearly at 100% of the plant N requirements and a PS and AN combination. Soil arylsulfatase and acid and alkaline phosphatase activities were measured at three different times in each growing season. The PS rate linearly increased the soil acid phosphatase activity in all 3 yr. In contrast, the alkaline phosphatase and arylsulfatase activities were enhanced in 1997 by the 8–16 Mg PS ha−1 treatments, whereas larger amounts of PS showed activity comparable to the control. The second PS application promoted phosphatase activities mostly in fall, but did not sustain arylsulfatase activity. The AN gave lower phosphatase activities than PS, and depressed arylsulfatase. Addition of AN to PS increased only acid phosphatase activity as compared with PS alone or the control. This study indicated that addition of PS improved enzyme activity of this horticultural soil but rates in excess to 32 Mg ha−1 may be detrimental. Key words: Papermill sludge, soil enzyme, cabbage, corn

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