scholarly journals Zinc-Ion-Dependent Acid Phosphatase Exhibits Magnesium-Ion-Dependent myo-Inositol-1-phosphatase Activity.

1996 ◽  
Vol 19 (6) ◽  
pp. 882-885 ◽  
Author(s):  
Sadaki FUJIMOTO ◽  
Isako OKANO ◽  
Yutaka TANAKA ◽  
Yasuo SUMIDA ◽  
Jyunji TSUDA ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Zinc Ion ◽  
Magnesium Ion ◽  
Inositol 1

Criteria for establishing a standardized method for determining alkaline phosphatase activity in human serum.

1977 ◽  
Vol 23 (12) ◽  
pp. 2263-2274 ◽  
Author(s):  
J P Bretaudière ◽  
A Vassault ◽  
L Amsellem ◽  
M L Pourci ◽  
H Thieu-Phung ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Human Serum ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Volume Fraction ◽  
Zinc Ion ◽  
Magnesium Ion ◽  
Ion Temperature ◽  
Nitrophenyl Phosphate ◽  
Standardized Method

Abstract We investigated factors influencing alkaline phosphatase activity in the course of developing criteria for the establishment of a standardized method for its determination in human serum at 30 degrees C. The effects of pH, phosphorylatable acceptor (2-amino-2-methyl-1-propanol and diethanolamine), 4-nitrophenyl phosphate, magnesium ion, zinc ion, temperature, volume fraction of specimen, and details of initiation of the reaction have been studied, with use of partly purified enzymes from bone, intestine, liver, and placenta, and sera from patients with a predominant characterized isoenzyme. The purity of the diethanolamine was examined and contaminant monoethanolamine was characterized as a competitive inhibitor. Two sets of recommended conditions are: 2-amino-2-methyl-1-propanol, 0.9 mol/liter; 4-nitrophenyl phosphate, 16 mmol/liter; magnesium ion, 1 mmol/liter; volume fraction of specimen 1/30, and pH30 degrees C 10.5; diethanolamine, 1.8 mol/liter; 4-nitrophenyl phosphate, 18 mmol/liter; magnesium ion, 1 mmol/liter; volume fraction of specimen 1/60, and pH30 degrees C 10.1. Serum is preincubated with all reagents but 4-nitrophenyl phosphate, which is used as the reaction-initiating substrate.

Erythrophagocytosis in the Liver in Hemolytic Anemias

1968 ◽  
Vol 26 ◽  
pp. 184-185
Author(s):  
O. T. Minick ◽  
E. Orfei ◽  
F. Volini ◽  
G. Kent
Keyword(s):  
Acid Phosphatase ◽  
Oxidative Damage ◽  
Phosphatase Activity ◽  
Kupffer Cells ◽  
Acid Phosphatase Activity ◽  
Common Type ◽  
Red Cell ◽  
Cell Fragments ◽  
Reticulo Endothelial System ◽  
Important Site

Hemolytic anemias were produced in rats by administering phenylhydrazine or anti-erythrocytic (rooster) serum, the latter having agglutinin and hemolysin titers exceeding 1:1000.Following administration of phenylhydrazine, the erythrocytes undergo oxidative damage and are removed from the circulation by the cells of the reticulo-endothelial system, predominantly by the spleen. With increasing dosage or if animals are splenectomized, the Kupffer cells become an important site of sequestration and are greatly hypertrophied. Whole red cells are the most common type engulfed; they are broken down in digestive vacuoles, as shown by the presence of acid phosphatase activity (Fig. 1). Heinz body material and membranes persist longer than native hemoglobin. With larger doses of phenylhydrazine, erythrocytes undergo intravascular fragmentation, and the particles phagocytized are now mainly red cell fragments of varying sizes (Fig. 2).

Tartrate-resistant acid phosphatase activity and glutathione levels are modulated during hFOB 1.19 osteoblastic differentiation

2008 ◽  
Vol 39 (6) ◽  
pp. 627-634 ◽  
Author(s):  
Tatiana Salles de Souza Malaspina ◽  
Célio Xavier dos Santos ◽  
Ana Paula Campanelli ◽  
Francisco Rafael Martins Laurindo ◽  
Mari Cleide Sogayar ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Osteoblastic Differentiation ◽  
Tartrate Resistant Acid Phosphatase
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