scholarly journals Potential inhibitors of rat tooth alkaline phosphatase studied by means of different histochemical techniques.

1979 ◽  
Vol 27 (5) ◽  
pp. 982-988 ◽  
Author(s):  
A Larsson ◽  
G Hasselgren
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Sodium Fluoride ◽  
Alkaline Phosphatase Activity ◽  
Staining Pattern ◽  
Alkaline Phosphatases ◽  
Phosphate Ion ◽  
Potential Inhibitors ◽  
Lead Pyrophosphate ◽  
Hydrolysis Of

Two histochemical methods for demonstration of alkaline phosphatase activity, a lead pyrophosphate- anda naphtholphosphate technique, were compared. Since different results may be due to methodological differences as well as different enzyme activities, the enzymatic hydrolysis of the naphtholphosphate was visualized both by means of an azo-dye coupler and by lead-capturing of the liberated phosphate ion. Various potential inhibitors of alkaline phosphatase activity (diphosphonate, D-penicillamine, and sodium fluoride) were also tested. The use of diphosphonate and D-penicillamine resulted in inhibited or reduced staining, which could mainly be explained by an interference by these compounds with components in the incubation media rather than with the enzyme itself. The addition of sodium fluoride had no effect on the naphtholphosphate staining pattern irrespective of capturing method, whereas the odontoblastic pyrophosphate splitting alkaline phosphatase appeared to be sensitive to sodium fluoride, suggesting the presence of two alkaline phosphatases in odontoblasts.

scholarly journals Alkaline Phosphatase Activity of Leukocytes in Shock

Blood ◽  
1955 ◽  
Vol 10 (7) ◽  
pp. 730-734 ◽  
Author(s):  
FRANCESCO VACCARI ◽  
BENITO SABOTTO ◽  
ENRICO MANZINI
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Alkaline Phosphatases ◽  
General Metabolism

Abstract In animals and patients subjected to stress procedures and shock, there occurs simultaneously with the increase in general metabolism a rise of the cytoplasmic localizations of the alkaline phosphatases in granulocytes.

scholarly journals A Comparison of Human Leukocyte Phosphatase Activity toward Sodium β-Glycerophosphate, Adenosine 5'-Phosphate and Glucose 1-Phosphate

Blood ◽  
1959 ◽  
Vol 14 (4) ◽  
pp. 415-422 ◽  
Author(s):  
JAMES H. FOLLETTE ◽  
WILLIAM N. VALENTINE ◽  
JOHN REYNOLDS
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Cell Population ◽  
Alkaline Phosphatase Activity ◽  
Human Leukocyte ◽  
Maximal Activity ◽  
Phosphate Esters ◽  
Chronic Myelocytic Leukemia ◽  
Myelocytic Leukemia ◽  
Hydrolysis Of

Abstract The ability of human leukocyte enzymes to hydrolyze phosphorus is compared in terms of the conventional substrate sodium β-glycerophosphate and the metabolically important phosphate esters, adenosine 5'-phosphate and glucose 1-phosphate. At pH 9.9, there is marked and comparable variation in phosphatase activity toward all three substrates, this being low in chronic myelocytic leukemia and high in the presence of infection and certain "stressful" states. Moreover, substrate mixture experiments show no increased hydrolysis of phosphorus when two substrates are present in the incubation mixture. Increased phosphatase activity toward both glucose 1-phosphate and sodium β-glycerophosphate resulted when corticosteroids were administered in large doses for 72 hours. The data, while not providing absolute proof, are compatible with the hydrolysis of phosphorus at pH 9.9, being due in the case of all three substrates to the activity of the same phosphomonoesterase or group of phosphomonesterases. At pH 5.5, phosphatase activity toward both sodium β-glycerophosphate and adenosine 5'-phosphate was likewise demonstrated, but, in leukocytes, the pH of maximal activity varies from subject to subject and is dependent to a large extent on the amount of the highly variable "alkaline phosphatase" activity present in any given cell population at the time of analysis.

Inhibition by concanavalin A as the basis for a specific assay of serum 5'-nucleotidase activity.

1977 ◽  
Vol 23 (12) ◽  
pp. 2311-2323 ◽  
Author(s):  
E R Zygowicz ◽  
F W Sunderman ◽  
E Horak ◽  
J F Dooley
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Concanavalin A ◽  
Significant Inhibition ◽  
Nucleotidase Activity ◽  
Hepatocellular Injury ◽  
Duct Ligation ◽  
The Difference ◽  
Hydrolysis Of

Abstract Concanavalin A inhibits serum 5'-nucleotidase activity, without causing significant inhibition of alkaline phosphatase activity. This observation serves as the basis for a new method for assaying the 5'-nucleotidase activity in serum, which depends upon the difference between the enzymic hydrolysis of adenosine-5'-monophosphate in the presence and absence of concanavalin A. A denosine released by the 5'-nucleotidase reaction is deaminated by a coupled reaction with adenosine deaminase to liberate inosine and ammonia, and ammonia is measured colorimetrically by the Berthelot reaction. In sera from 40 healthy adult persons, 5'-nucleotidase activity averaged 6.4 U/liter (SD, +/-2.0; range, 3-12). In sera from 100 patients, measurements of 5'-nucleotidase activity by the new assay averaged 8% lower than by a generally accepted method in which phenyl phosphate is used to suppress hydrolysis of adenosine-5'-monophosphate by alkaline phosphatase activity. The clinical validy of the new assay was tested by measuring serum 5'-nucleotidase activities in rats with bile duct ligation and in rats treated with thioacetamide to induce hepatocellular injury.

Influence of Light on the Alkaline Phosphatase Activity of Selenastrum capricornutum (Chlorophyceae) in Streams

1985 ◽  
Vol 42 (2) ◽  
pp. 384-388 ◽  
Author(s):  
R. L. Klotz
Keyword(s):  
New York ◽  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
New York State ◽  
Selenastrum Capricornutum ◽  
Alkaline Phosphatases ◽  
Reactive Phosphorus ◽  
First Time

The alkaline phosphatase activity (APA) of Selenastrum capricomutum Printz incubated in situ in four streams in New York State was inversely related to total insolation. APA was not correlated with stream molybdate reactive phosphorus over the range of concentrations encountered. Selenastrum showed no diel cycle of APA. The phosphorus fraction made available by the activity of alkaline phosphatases, enzyme hydrolyzable phosphorus (measured for the first time in streams), increased the phosphorus supply to organisms with high APA.

LEUCOCYTE METABOLISM IN PREGNANCY

1960 ◽  
Vol XXXV (IV) ◽  
pp. 575-584 ◽  
Author(s):  
C. Borel ◽  
J. Frei ◽  
A. Vannotti
Keyword(s):  
Alkaline Phosphatase ◽  
Oxygen Consumption ◽  
Pregnant Women ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Lactate Production ◽  
Glucose Consumption ◽  
In Pregnancy

ABSTRACT Enzymatic studies, on leucocytes of pregnant women, show an increase of the alkaline phosphatase activity and a decrease of the glucose consumption and lactate production, as well as of proteolysis. The oxygen consumption, with succinate as substrate, does not vary.

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