Activity coefficients of electrolyte and amino acid in the systems (water + potassium chloride +dl -valine) at T=298.15 K and (water + sodium chloride +l -valine) at T= 308.15 K

2002 ◽  
Vol 34 (8) ◽  
pp. 1297-1309 ◽  
Author(s):  
A. Khavaninzadeh ◽  
H. Modarress ◽  
V. Taghikhani ◽  
M.K. Khoshkbarchi

2011 ◽  
Vol 2011 ◽  
pp. 1-5
Author(s):  
Jessica Kopf ◽  
Daniel Hormigo ◽  
José Luis García ◽  
Carmen Acebal ◽  
Isabel de la Mata ◽  
...  

Inhibition of recombinant D-amino acid oxidase from Trigonopsis variabilis (TvDAAO) activity in the presence of different sodium salts and potassium chloride is reported. A competitive inhibition pattern by sodium chloride was observed, and an inhibition constant value of Ki=85 mM was calculated. Direct connection of NaCl inhibition with FAD cofactor dissociation was confirmed by measuring the fluorescence of tryptophanyl residues of the holoenzyme.



1981 ◽  
Vol 46 (12) ◽  
pp. 3104-3109 ◽  
Author(s):  
Miroslav Ludwig ◽  
Oldřich Pytela ◽  
Miroslav Večeřa

Rate constants of non-catalyzed hydrolysis of 3-acetyl-1,3-diphenyltriazene (I) and 3-(N-methylcarbamoyl)-1,3-diphenyltriazene (II) have been measured in the presence of salts (ammonium chloride, potassium chloride, lithium chloride, sodium chloride and bromide, ammonium sulphate, potassium sulphate, lithium sulphate, sodium sulphate and zinc sulphate) within broad concentration ranges. Temperature dependence of the hydrolysis of the substrates studied has been measured in the presence of lithium sulphate within temperature range 20° to 55 °C. The results obtained have been interpreted by mechanisms of hydrolysis of the studied substances.





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