scholarly journals Inactivation of phosphorylase b by potassium ferrate, a new reactive analogue of the phosphate group.

1976 ◽  
Vol 251 (6) ◽  
pp. 1553-1560
Author(s):  
Y M Lee ◽  
W F Benisek
Keyword(s):  
Phosphate Group ◽  
Potassium Ferrate

Viral inactivation by potassium ferrate

1995 ◽  
Vol 31 (5-6) ◽  
pp. 165-168 ◽  
Author(s):  
Futaba Kazama
Keyword(s):  
Phosphate Buffer ◽  
Potassium Ferrate ◽  
Sodium Thiosulphate ◽  
Viral Inactivation ◽  
Complete Decomposition ◽  
Kinetics Of ◽  
Oxidative Intermediate

The kinetics of inactivation by potassium ferrate were studied using a bacteriophage, F-specific RNA-coliphage Qβ as a viral model. The inactivation appeared to be expressed by Hom's model in phosphate buffer at pH 6, 7, and 8. The rate of inactivation depended on pH; the lower pH, the faster inactivation observed. To consider the mechanism by which ferrate caused inactivation, the efficiency of inactivation was checked after ferrate decomposition in buffer. Effective inactivation following Hom's model was also observed after the complete decomposition of ferrate ion; however, the efficiency of that inactivation disappeared by the addition of sodium thiosulphate, suggesting that rather long-lived oxidative intermediate was generated by the decomposition of ferrate ion. The intermediate might take part in the inactivation.

The effect of acceptor modification upon the synthesis of dinucleoside phosphates catalyzed by non-specific ribonucleases of Penicillium claviforme

1979 ◽  
Vol 44 (2) ◽  
pp. 613-625 ◽  
Author(s):  
Valentina I. Gulyaeva ◽  
Antonín Holý
Keyword(s):  
Reaction Center ◽  
Hydroxy Group ◽  
Pyrimidine Ring ◽  
Phosphate Group ◽  
Mutual Orientation ◽  
Acceptor Molecule ◽  
Heterocyclic Base ◽  
Sugar Moiety ◽  
Cyclic Phosphate ◽  
Penicillium Claviforme

The present paper studies the effect of the modification of heterocyclic base, sugar moiety and the presence of phosphate group on the nucleoside acceptors in the synthesis of dinucleoside phosphates from adenosine 2',3'-cyclic phosphate as donor, catalyzed by nonspecific acidic extracellular and intracellular ribonucleases from Penicillium claviforme. The enzyme binds specifically the acceptor molecule, preferring cytosine nucleosides. It requires the presence of the whole sugar moiety, an exact mutual orientation of the heterocyclic base and the reaction center (5'-hydroxy group), and a suitable conformation of the acceptor molecule. The enzyme-acceptor bond is homochiral and the presence of the N3-H group in the pyrimidine ring is important. The reaction between the donor and the acceptor is bimolecular and is competitively inhibited by some purine nucleosides.

Simultaneous Degradation of Cu(II) and Cr(VI) in the Micro-Polluted Water by Potassium Ferrate

2013 ◽  
Vol 295-298 ◽  
pp. 1191-1194
Author(s):  
Lei Zhang ◽  
Zhao Cheng Zhang ◽  
Jian Guo Cui
Keyword(s):  
Degradation Mechanism ◽  
Synergetic Effect ◽  
Oxidation Time ◽  
Polluted Water ◽  
Potassium Ferrate ◽  
Experiment Study ◽  
Removal Rates ◽  
Degradation Effect ◽  
Flocculation Time ◽  
Simultaneous Degradation

This Experiment study on the simultaneous degradation effect of Cu(II) and Cr(Ⅵ) in the micro-polluted water by potassium ferrate. And the influential elements on the removal effects and probed into the degradation mechanism was analyzed. The results indicated that the removal rates of Cu(II),Cr(Ⅵ) by synergetic effect of potassium ferrate oxidation and coagulation were 76.2%、62.2%,respectively,when the optimizing conditions were as follows: oxidation pH was 7,oxidation time was 20min,flocculation pH was 9,flocculation time was 30min and dosage of potassium ferrate was 40mg/L.

The Stability of Potassium Ferrate in Water

2014 ◽  
Vol 881-883 ◽  
pp. 215-218
Author(s):  
Kai Luo ◽  
Gang Cao ◽  
Ming Yu Li ◽  
Gang Ren
Keyword(s):  
Influencing Factors ◽  
Potassium Ferrate ◽  
The Stability

The influencing factors of the stability for the potassium ferrate (K2FeO4), including pH, alkalinity, O3, KI, KClO3, KCl, NaClO3and Na2SiO3, were studied in this work. The results showed that the K2FeO4stability in water is best at about pH=10. The higher the alkalinity is, the stronger of K2FeO4stability would be. The O3had no effect to improve the K2FeO4stability. The K2FeO4stability would be best in water with 15mmol/L NaClO3, 10mmol/L Na2SiO3and 9mol/L alkalinity. Under this condition, the K2FeO4content would be 83.28% after 24h.

scholarly journals INTRODUCTION OF PHOSPHATE GROUP INTO β-ARBUTIN BY CYCLO-TRIPHOSPHATE

2017 ◽  
Vol 33 (0) ◽  
pp. 21-25
Author(s):  
Hideko Maeda ◽  
Mako Katsushiro ◽  
Hiroyuki Nariai ◽  
Hirokazu Nakayama
Keyword(s):  
Phosphate Group
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