A Critical Study of Techniques for Determining the Cytological position of Alkaline Phosphatase

1946 ◽  
Vol 22 (3-4) ◽  
pp. 110-117
Author(s):  
J. F. DANIELLI
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Critical Time ◽  
Phosphate Esters ◽  
Critical Study ◽  
Brush Borders ◽  
Glomerular Filtrate ◽  
Alternative Techniques ◽  
Selection Of

1. It has been proved that the technique of Takamatsu and Gömorri indicates the cytological sites of alkaline phosphatase activity. 2. The critical time limits for the various operations in the technique have been determined. 3. Several alternative techniques are given for demonstrating phosphatase activity on the cytological level. 4. A selection of fixatives is given which do not produce severe destruction of alkaline phosphatase activity. 5. It has been shown that alkaline phosphatase in fixed perparations is found in sites which are those in which it occurs under physiological conditions. 6. It is suggested that the function of the phosphatase found in the brush borders of the proximal tubules of the kidney is to hydrolyse phosphate esters in the glomerular filtrate, and thereby permit the reabsorption of the component molecules by tubular processes.

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.

Measurement of alkaline phosphatase activity by electrochemical detection of phosphate esters

1989 ◽  
Vol 266 (2) ◽  
pp. 309-316 ◽  
Author(s):  
Jane E. Frew ◽  
Nicola C. Foulds ◽  
Jane M. Wilshere ◽  
Nigel J. Forrow ◽  
Monika J. Green
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Electrochemical Detection ◽  
Alkaline Phosphatase Activity ◽  
Phosphate Esters

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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