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.

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.

scholarly journals Origin of an Elevated Plasma Alkaline Phosphatase Activity in Non-Jaundiced Patients

1978 ◽  
Vol 15 (1-6) ◽  
pp. 86-90 ◽  
Author(s):  
H. J. W. Cleeve
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Nucleotidase Activity ◽  
Elevated Plasma ◽  
Phosphatase Activities ◽  
Alkaline Phosphatase Isoenzymes ◽  
Effect Of Treatment ◽  
Plasma Alkaline Phosphatase ◽  
Alkaline Phosphatase Isoenzyme

Summary Samples from 260 non-jaundiced patients with elevated plasma alkaline phosphatase activities were analysed for γ-glutamyltransferase and 5′-nucleotidase activity, and for alkaline phosphatase isoenzyme pattern. The plasma γ-glutamyltransferase activity was found to be a more sensitive index than that of plasma 5′-nucleotidase in confirming the presence of a liver component of the elevated plasma alkaline phosphatase. If the γ-glutamyltransferase level is normal it is probable that the increase in plasma alkaline phosphatase activity is of bone origin. However, an elevated γ-glutamyltransferase result does not exclude a bone component; in this situation plasma alkaline phosphatase isoenzymes should be estimated. The causes of elevated activities of plasma alkaline phosphatase, 5′-nucleotidase and γ-glutamyltransferase, found in this investigation were generally the same as those found by other workers. The effect of treatment by drugs on γ-glutamyltransferase, an inducible enzyme, needs more investigation.

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.

The mechanism of elevated alkaline phosphatase activity after bile duct ligation in the rat

Hepatology ◽  
1986 ◽  
Vol 6 (3) ◽  
pp. 374-380 ◽  
Author(s):  
Shakuntla Seetharam ◽  
Norman L. Sussman ◽  
Tsugikazu Komoda ◽  
David H. Alpers
Keyword(s):  
Alkaline Phosphatase ◽  
Bile Duct ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Bile Duct Ligation ◽  
Elevated Alkaline Phosphatase ◽  
Duct Ligation

Fluorometric and colorimetric analysis of alkaline phosphatase activity based on a nucleotide coordinated copper ion mimicking polyphenol oxidase

2019 ◽  
Vol 7 (42) ◽  
pp. 6508-6514 ◽  
Author(s):  
Hui Huang ◽  
Juan Bai ◽  
Jiao Li ◽  
Lulu Lei ◽  
Wenjing Zhang ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Catalytic Activity ◽  
Phosphatase Activity ◽  
Polyphenol Oxidase ◽  
Alkaline Phosphatase Activity ◽  
Detection Method ◽  
Colorimetric Detection ◽  
Copper Ion ◽  
Colorimetric Analysis ◽  
The Difference

We have established a fluorometric and colorimetric detection method for alkaline phosphatase based on the difference in the catalytic activity of polyphenol oxidase mimetic enzymes formed by a nucleotide coordinated copper ion.

Studies on the unmasking of membrane-bound alkaline phosphatase during the differentiation of Dictyostelium discoideum

1984 ◽  
Vol 62 (10) ◽  
pp. 970-974 ◽  
Author(s):  
D. V. Mohan Das ◽  
Gerald Weeks
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Dictyostelium Discoideum ◽  
Alkaline Phosphatase Activity ◽  
Developmental Regulation ◽  
Nucleotidase Activity ◽  
Nitrophenyl Phosphate ◽  
Single Protein ◽  
Membrane Bound ◽  
Triton X

Evidence has been presented recently to suggest that the 5′-nucleotidase and alkaline phosphatase activities of culmination phase cells of Dictyostelium discoideum are due to a single protein. However, we find that the membrane bound 5′-nucleotidase activity is only marginally activated by either 50 °C treatment or by dialysis, conditions that markedly activate alkaline phosphatase activity. In contrast, the 5′-nucleotidase activity of Triton X-100 extracts is activated by dialysis to the same extent as alkaline phosphatase activity. The available evidence suggests that, although a single protein is responsible for both alkaline phosphatase and 5′-nucleotidase activities, the characteristics of binding of the two substrates p-nitrophenyl phosphate and AMP to this enzyme are somewhat different. The alkaline phosphatase activity of dialyzed vegetative cell membranes is inhibited by the addition of concentrated dialyzate and this inhibition is reversed by further dialysis. The culmination phase enzyme is also inhibited by concentrated dialyzate from vegetative cells, suggesting that the removal of inhibitor from the enzyme can completely account for the developmental regulation. Dialyzates from culmination phase membranes do not inhibit enzyme activity, indicating the absence of inhibitor in these preparations. Alkaline phosphatase and 5′-nucleotidase activities of a partially purified enzyme preparation are equally inhibited by the addition of the concentrated dialyzate.

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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