Arylsulfatase and alkaline phosphatase (APASE) activity in sediments of Lake Kinneret, Israel

1997 ◽  
Vol 99 (1-4) ◽  
pp. 671-679 ◽  
Author(s):  
O. Riadas ◽  
R. Pinkas
Keyword(s):  
Alkaline Phosphatase ◽  
Lake Kinneret ◽  
Apase Activity

ALKALINE PHOSPHATASE ACTIVITY ASSOCIATED WITH THE WALLS OF DIFFERENT ORGANS OF THE GASTROINTESTINAL TRACT IN NEWBORN, YOUNG AND YEARLING BOVINES: EFFECTS OF DIET AND FASTING

1981 ◽  
Vol 61 (2) ◽  
pp. 311-318 ◽  
Author(s):  
J. P. FAY ◽  
K.-J. CHENG ◽  
J. W. COSTERTON
Keyword(s):  
Alkaline Phosphatase ◽  
Statistical Analysis ◽  
Gastrointestinal Tract ◽  
Alkaline Phosphatase Activity ◽  
Absorption Capacity ◽  
The Other ◽  
Tissue Samples ◽  
Holstein Calves ◽  
Newborn Calves ◽  
Apase Activity

Alkaline phosphatase (APase) activity was assayed in tissue samples from the gastrointestinal tract (GIT) of newborn Holstein calves, and of 3- to 10-mo-old calves fed on milk only or starter-grower ration plus alfalfa hay. Statistical analysis of APase activity from different regions of the GIT showed effects of diet and site (P < 0.01) and an interaction of diet × site (P < 0.01) on APase activity. APase was high in the reticulo-rumen: intermediate in the omasum and the intestinal region: and low in the tongue, esophagus and abomasum. Within the same organ. APase differed considerably according to the location of the sites. Calves fed the fiber-containing diet had higher APase than those fed milk only. APase activity in the reticulo-rumen was much lower in newborn calves than in older calves, but in the other regions of the GIT, values were similar for the two groups. The effect of fasting on APase activity in rumen and abomasum walls of 20 yearling Hereford and Angus bulls fed on two different diets was also studied. In most cases, fasting decreased wall-associated APase activities. Interactions for breed × diet × site (P < 0.01), for breed × fasting × site (P < 0.01), and for diet × fasting × site (P < 0.05) on rumen APase activity, and for breed × diet × fasting (P < 0.01) on abomasum APase activity, were detected in this experiment. These variations in APase activity within the digestive tract are discussed in relation to the absorption capacity, degree of abrasion, and degree of keratinization of the tissues involved.

scholarly journals A novel fluorogenic substrate for detecting alkaline phosphatase activity in situ.

1993 ◽  
Vol 41 (2) ◽  
pp. 313-317 ◽  
Author(s):  
Z Huang ◽  
W You ◽  
R P Haugland ◽  
V B Paragas ◽  
N A Olson ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Cell Line ◽  
Egf Receptor ◽  
Egf Receptors ◽  
Fluorogenic Substrate ◽  
Epidermal Growth ◽  
In Situ Detection ◽  
Apase Activity ◽  
Human Epidermoid Carcinoma

We describe here the in situ detection of alkaline phosphatase (APase) activity with a new fluorogenic substrate, 2-(5'-chloro-2'-phosphoryloxyphenyl)-6-chloro-4-(3H)-quinazolinone (CPPCQ). CPPCQ is very soluble and colorless. APase converts it into a rapidly precipitating product, whose strong fluorescence marks the sites of APase activity. The detected APase was either a probing enzyme anchored to epidermal growth factor (EGF) receptors of fixed human epidermoid carcinoma cell line (A431) by biotinylated EGF and streptavidin-APase conjugates or an endogenous marker existing in a fixed canine kidney cell line (MDCK). With CPPCQ staining, the EGF receptors and the endogenous APase were both visualized by fluorescence microscopy as contrasting, photostable, and well-resolved fluorescent stains. The EGF receptor staining was specific since it could be blocked by excessive unlabeled EGF. In contrast, fluorescein-labeled EGF failed to specifically stain the EGF receptors under the same fluorescent microscope. The endogenous APase staining with CPPCQ was sensitive to heating, levamisole and L-homoarginine, showing an APase tissue specificity of the liver/bone/kidney type. Therefore, CPPCQ appears to be a novel substrate dye for sensitive fluorescence APase histochemistry.

The constitutive nature of alkaline phosphatase in rumen bacteria

1980 ◽  
Vol 26 (2) ◽  
pp. 268-272 ◽  
Author(s):  
C. W. Forsberg ◽  
K.-J. Cheng
Keyword(s):  
Alkaline Phosphatase ◽  
Batch Culture ◽  
Culture Medium ◽  
Rumen Fluid ◽  
Inorganic Phosphorus ◽  
Phosphorus Concentration ◽  
Rumen Bacteria ◽  
Megasphaera Elsdenii ◽  
Rumen Microflora ◽  
Apase Activity

Alkaline phosphatase (APase) activity of Megasphaera elsdenii was enhanced by PO42− limitation in batch culture; however, six other species of rumen bacteria tested showed no increase in APase activity under these conditions. Alkaline phosphatase was produced by the mixed rumen microflora even though the inorganic phosphorus concentration was as high as 10 mM. The APase activity of the bacterial fraction from rumen fluid was not increased during incubation in a phosphorus-free culture medium. Since bacteria may account for greater than 80% of the APase activity in the rumen, this would suggest that the bulk of the APase activity in the rumen is synthesized constitutively. The bacterium responsible for most of the APase activity probably is Bacteroides ruminicola.

UV irradiation of a B-cell hybridoma increases expression of alkaline phosphatase: involvement in apoptosis

1997 ◽  
Vol 75 (6) ◽  
pp. 783-788 ◽  
Author(s):  
Vongthip Souvannavong ◽  
Christophe Lemaire ◽  
Spencer Brown ◽  
Arlette Adam
Keyword(s):  
Flow Cytometry ◽  
Alkaline Phosphatase ◽  
B Cell ◽  
Uv Irradiation ◽  
Ultraviolet Irradiation ◽  
Specific Inhibitor ◽  
Apoptotic Cells ◽  
Fast Red ◽  
Irradiation Cell ◽  
Apase Activity

Expression of alkaline phosphatase (APase) by 7TD1 B-cell hybridoma was amplified by ultraviolet irradiation; cell growth was inhibited and cell death by apoptosis was increased. Irradiation induced high levels of APase activity in cycling as well as in apoptotic cells. In contrast, APase activity faded with time in nonirradiated cells and was no longer expressed in spontaneous apoptotic cells appearing after several days in culture. This was demonstrated by cell morphology, DNA fragmentation, and flow cytometry after simultaneous staining of DNA with Hoechst 33342 and APase with naphthol AS-TR phosphate - fast red RC fluorescent reagent. Levamisole, a specific inhibitor of APase activity, almost totally abrogated apoptosis induced by ultraviolet irradiation at doses that failed to affect 7TD1 cell survival. These data suggest that APase could play a role in the signalling cascade that mediates apoptosis in irradiated cells. Key words: alkaline phosphatase, apoptosis, flow cytometry, levamisole, UV irradiation.

Interrelationship of the cellular distribution and secretion of regular structure (RS) protein in Bacillus licheniformis nm 105

1992 ◽  
Vol 50 (1) ◽  
pp. 712-713
Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh
Keyword(s):  
Alkaline Phosphatase ◽  
Bacillus Licheniformis ◽  
Self Assembly ◽  
Gel Electrophoresis ◽  
Culture Supernatant ◽  
Regular Structure ◽  
The Self ◽  
Cellular Distribution ◽  
Structural Protein ◽  
Laboratory Cultures

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.

In Situ Localization of PPAR Gamma and Uncoupling Protein in Mouse Embryo Sections Using Digoxigenin-Labeled Riboprobes

1996 ◽  
Vol 54 ◽  
pp. 32-33
Author(s):  
C. Jennermann ◽  
S. A. Kliewer ◽  
D. C. Morris
Keyword(s):  
Alkaline Phosphatase ◽  
Room Temperature ◽  
Uncoupling Protein ◽  
Ppar Gamma ◽  
Nuclear Hormone Receptor ◽  
Full Length ◽  
Northern Analysis ◽  
Peroxisome Proliferator

Peroxisome proliferator-activated receptor gamma (PPARg) is a member of the nuclear hormone receptor superfamily and has been shown in vitro to regulate genes involved in lipid metabolism and adipocyte differentiation. By Northern analysis, we and other researchers have shown that expression of this receptor predominates in adipose tissue in adult mice, and appears first in whole-embryo mRNA at 13.5 days postconception. In situ hybridization was used to find out in which developing tissues PPARg is specifically expressed.Digoxigenin-labeled riboprobes were generated using the Genius™ 4 RNA Labeling Kit from Boehringer Mannheim. Full length PPAR gamma, obtained by PCR from mouse liver cDNA, was inserted into pBluescript SK and used as template for the transcription reaction. Probes of average size 200 base pairs were made by partial alkaline hydrolysis of the full length transcripts. The in situ hybridization assays were performed as described previously with some modifications. Frozen sections (10 μm thick) of day 18 mouse embryos were cut, fixed with 4% paraformaldehyde and acetylated with 0.25% acetic anhydride in 1.0M triethanolamine buffer. The sections were incubated for 2 hours at room temperature in pre-hybridization buffer, and were then hybridized with a probe concentration of 200μg per ml at 70° C, overnight in a humidified chamber. Following stringent washes in SSC buffers, the immunological detection steps were performed at room temperature. The alkaline phosphatase labeled, anti-digoxigenin antibody and detection buffers were purchased from Boehringer Mannheim. The sections were treated with a blocking buffer for one hour and incubated with antibody solution at a 1:5000 dilution for 2 hours, both at room temperature. Colored precipitate was formed by exposure to the alkaline phosphatase substrate nitrobluetetrazoliumchloride/ bromo-chloroindlylphosphate.

Electron microscopic study of the membrane glycoproteins in the rat kidney after cisplatin treatment

1989 ◽  
Vol 47 ◽  
pp. 912-913
Author(s):  
S.K. Aggarwal
Keyword(s):  
Alkaline Phosphatase ◽  
Rat Kidney ◽  
Light And Electron Microscopy ◽  
Kidney Tissue ◽  
Membrane Glycoproteins ◽  
Electron Microscopic ◽  
Before And After ◽  
Interstrand Cross Links ◽  
Cross Links

The proposed primary mechanism of action of the anticancer drug cisplatin (Cis-DDP) is through its interaction with DNA, mostly through DNA intrastrand cross-links or DNA interstrand cross-links. DNA repair mechanisms can circumvent this arrest thus permitting replication and transcription to proceed. Various membrane transport enzymes have also been demonstrated to be effected by cisplatin. Glycoprotein alkaline phosphatase was looked at in the proximal tubule cells before and after cisplatin both in vivo and in vitro for its inactivation or its removal from the membrane using light and electron microscopy.Outbred male Swiss Webster (Crl: (WI) BR) rats weighing 150-250g were given ip injections of cisplatin (7mg/kg). Animals were killed on day 3 and day 5. Thick slices (20-50.um) of kidney tissue from treated and untreated animals were fixed in 1% buffered glutaraldehyde and 1% formaldehyde (0.05 M cacodylate buffer, pH 7.3) for 30 min at 4°C. Alkaline phosphatase activity and carbohydrates were demonstrated according to methods described earlier.

Serum Alkaline Phosphatase in Liver Disease: A Concept of its Significance

1950 ◽  
Vol 16 (4) ◽  
pp. 660-668 ◽  
Author(s):  
James O. Burke
Keyword(s):  
Alkaline Phosphatase ◽  
Liver Disease ◽  
Serum Alkaline Phosphatase

The Origin of Elevation of Serum Alkaline Phosphatase in Hepatic Disease

1962 ◽  
Vol 42 (4) ◽  
pp. 431-438 ◽  
Author(s):  
Stanton G. Polin ◽  
Mitchell A. Spellberg ◽  
Lloyd Teitelman ◽  
Makoto Okumura
Keyword(s):  
Alkaline Phosphatase ◽  
Serum Alkaline Phosphatase ◽  
Hepatic Disease
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