Real-Time Colorimetric Assay of Inorganic Pyrophosphatase Activity Based on Reversibly Competitive Coordination of Cu2+between Cysteine and Pyrophosphate Ion

2013 ◽  
Vol 85 (19) ◽  
pp. 9409-9415 ◽  
Author(s):  
Jingjing Deng ◽  
Qin Jiang ◽  
Yuexiang Wang ◽  
Lifen Yang ◽  
Ping Yu ◽  
...  
Keyword(s):  
Real Time ◽  
Colorimetric Assay ◽  
Inorganic Pyrophosphatase ◽  
Competitive Coordination ◽  
Pyrophosphatase Activity

Monitoring inorganic pyrophosphatase activity with the fluorescent dizinc(ii) complex of a macrocycle bearing one dansylamidoethyl antenna

2020 ◽  
Vol 49 (27) ◽  
pp. 9487-9494 ◽  
Author(s):  
Ana Cruz ◽  
Ara Núñez-Montenegro ◽  
Pedro Mateus ◽  
Rita Delgado
Keyword(s):  
Real Time ◽  
Inorganic Pyrophosphatase ◽  
Pyrophosphatase Activity

The dizinc(ii) complex of a hexaazamacrocycle with an antenna allowed monitoring of the PPi hydrolysis by using inorganic pyrophosphatase in real-time.

Method for Real-Time Detection of Inorganic Pyrophosphatase Activity

2001 ◽  
Vol 293 (1) ◽  
pp. 67-70 ◽  
Author(s):  
Jonas Eriksson ◽  
Samer Karamohamed ◽  
Pål Nyrén
Keyword(s):  
Real Time ◽  
Inorganic Pyrophosphatase ◽  
Pyrophosphatase Activity ◽  
Real Time Detection

Real-time assay of inorganic pyrophosphatase activity in the red region based on Li+-doped NaYF4:Yb,Er upconversion luminescent nanoparticles

2017 ◽  
Vol 9 (22) ◽  
pp. 3296-3301 ◽  
Author(s):  
Lei Wang ◽  
Yuan Ji ◽  
Yuezhen He ◽  
Lun Wang ◽  
Hongqi Chen
Keyword(s):  
Real Time ◽  
Inorganic Pyrophosphatase ◽  
Competition Assay ◽  
Highly Sensitive ◽  
Luminescent Nanoparticles ◽  
Pyrophosphatase Activity ◽  
Real Time Detection ◽  
Sensitive Method

Based on a competition assay approach, a new highly sensitive method for real-time detection of PPase activity using Li+-doped NaYF4:Yb,Er upconversion red luminescent nanoparticles was developed.

Inorganic Pyrophosphatase Activity of Purified Bovine Pulp Alkaline Phosphatase at Physiological pH

1986 ◽  
Vol 65 (2) ◽  
pp. 125-127 ◽  
Author(s):  
M. Harada ◽  
N. Udagawa ◽  
K. Fukasawa ◽  
B.Y. Hiraoka ◽  
M. Mogi
Keyword(s):  
Alkaline Phosphatase ◽  
Inorganic Pyrophosphatase ◽  
Pyrophosphatase Activity

THE METABOLISM OF THE ERYTHROCYTE: X. THE INORGANIC PYROPHOSPHATASE OF THE ERYTHROCYTE

1956 ◽  
Vol 34 (1) ◽  
pp. 121-129 ◽  
Author(s):  
A. Malkin ◽  
O. F. Denstedt
Keyword(s):  
Enzyme Activity ◽  
Calcium Ions ◽  
Human Erythrocyte ◽  
Inorganic Pyrophosphatase ◽  
Magnesium Ions ◽  
Constant Ratio ◽  
Inorganic Pyrophosphate ◽  
Noncompetitive Inhibitor ◽  
Pyrophosphatase Activity ◽  
Hydrolysis Of

The activity of the pyrophosphatase which catalyzes the hydrolysis of inorganic pyrophosphate in the erythrocyte of the human, the rabbit, and the chicken is confined entirely to the cytoplasm of the cell. Following preincubation, the enzyme activity in the human erythrocyte is diminished, but pre-incubation in the presence of cysteine or glutathione prevents the diminution of the enzyme activity. Aging of the hemolyzate of the human erythrocytes results in a marked loss of the inorganic pyrophosphatase activity. The diminished activity can be restored by the addition of cysteine or glutathione to the reaction mixture; but after the hemolyzate has aged for five or six days at 5 °C, the loss in the enzyme activity can no longer be restored with these reagents. Fluoride and calcium ions inhibit the activity of the enzyme, while magnesium ions are essential for its activity. Calcium is a noncompetitive inhibitor, while the inhibition by fluoride is of a "quadratic" nature. If a constant ratio of magnesium to pyrophosphate is maintained, the quadratic inhibition can be converted to the "uncompetitive" type of inhibition.

Inorganic pyrophosphatases in leaves during plant development and senescence

1971 ◽  
Vol 49 (2) ◽  
pp. 311-316 ◽  
Author(s):  
W. E. Rauser
Keyword(s):  
Leaf Age ◽  
Maximum Level ◽  
Inorganic Pyrophosphatase ◽  
Leucine Incorporation ◽  
Biosynthetic Activity ◽  
Delayed Senescence ◽  
Plant Parts ◽  
Leaf Tissues ◽  
Pyrophosphatase Activity ◽  
Alkaline Activity

The activities of inorganic pyrophosphatases were determined in developing and senescing leaf tissues as indicators of biosynthetic activity. The level of alkaline inorganic pyrophosphatase varied with leaf age and leaf position on the plant. In younger plants alkaline inorganic pyrophosphatase increased up the plant to a maximum and then decreased with leaf proximity to the apex. In older plants the enzymatic activity decreased in the lower leaves and the maximum level occurred in leaves closer to the apex. Retardation of leaf senescence with benzyladenine maintained the high levels of enzyme activity. In cucumber plants removal of the shoot at any time before cotyledon death rejuvenated the cotyledons leading to excessive growth, regreening, and dramatic increases in alkaline inorganic pyrophosphatase. Alkaline inorganic pyrophosphatase activity correlated highly with 14C-leucine incorporation into protein of bean leaf discs, supporting the view that this enzyme is involved in making biosynthetic pathways irreversibly anabolic. Acid inorganic pyrophosphatase activity was not proportional to the alkaline activity, suggesting that two separate enzymatic proteins are being assayed. It is concluded that the level of alkaline inorganic pyrophosphatase can be used to indicate which plant parts have high biosynthetic capacity. Also, delayed senescence of leaves or cotyledons, with benzyladenine or apex excision, is associated with maintained biosynthesis.

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