Removal of Co2+and Sr2+from a Primary Coolant by Continuous Electrodeionization Packed with Weak Base Anion Exchange Resin

2010 ◽  
Vol 172 (1) ◽  
pp. 71-76 ◽  
Author(s):  
Fu-Zhi Li ◽  
Meng Zhang ◽  
Xuan Zhao ◽  
Tao Hou ◽  
Li-Jun Liu
Keyword(s):  
Anion Exchange ◽  
Exchange Resin ◽  
Anion Exchange Resin ◽  
Weak Base ◽  
Primary Coolant ◽  
Weak Base Anion Exchange

Separation of Boron from Geothermal Water Using a Boron Selective Macroporous Weak Base Anion Exchange Resin

2010 ◽  
Vol 45 (6) ◽  
pp. 809-813 ◽  
Author(s):  
Idil Yilmaz-Ipek ◽  
Pelin Koseoglu ◽  
Umran Yuksel ◽  
Nazlı Yasar ◽  
Gözde Yolseven ◽  
...  
Keyword(s):  
Anion Exchange ◽  
Exchange Resin ◽  
Anion Exchange Resin ◽  
Geothermal Water ◽  
Weak Base ◽  
Weak Base Anion Exchange

Kinetic modeling and error analysis for zinc removal on a weak base anion exchange resin

2015 ◽  
Vol 57 (41) ◽  
pp. 19510-19518 ◽  
Author(s):  
Emilia Gîlcă ◽  
Andrada Măicăneanu ◽  
Adina Ghirişan ◽  
Petru Ilea
Keyword(s):  
Error Analysis ◽  
Anion Exchange ◽  
Kinetic Modeling ◽  
Exchange Resin ◽  
Anion Exchange Resin ◽  
Weak Base ◽  
Zinc Removal ◽  
Weak Base Anion Exchange

THE WHEAT LEAF PHOSPHATASES: VIII. A PREPARATION WITH PHOSPHOTRANSFERASE ACTIVITY

1967 ◽  
Vol 45 (3) ◽  
pp. 401-408 ◽  
Author(s):  
D. W. A. Roberts
Keyword(s):  
Anion Exchange ◽  
Exchange Resin ◽  
Anion Exchange Resin ◽  
Weak Base ◽  
Low Level ◽  
Wheat Leaf ◽  
Nucleoside Phosphotransferase ◽  
Wheat Leaves ◽  
Weak Base Anion Exchange ◽  
Acid Phosphomonoesterase

The nucleoside phosphotransferase of wheat leaves has been separated from the acid β-glycerophosphatase (EC 3.1.3.2) by chromatography on the weak base anion exchange resin Rexyn 203. The preparation is contaminated with 3′-nucleotidase (EC 3.1.3.6), acid pyrophosphatase (EC 3.6.1.1), and a phosphotransferase that apparently catalyzes the interconversion of adenosine 3′-phosphate and adenosine 5′-phosphate. The low level of acid β-glycerophosphatase activity in these preparations proves the existence of an active acid pyrophosphatase in wheat leaves that is distinct from classical acid phosphomonoesterase, which is supposed to hydrolyze pyrophosphate.

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