Thermodynamic characteristics of molecular interactions between L-tryptophan and nicotinic acid and uracyl in aqueous buffer solutions at 298 K

2015 ◽  
Vol 89 (12) ◽  
pp. 2229-2233 ◽  
Author(s):  
V. G. Badelin ◽  
E. Yu. Tyunina ◽  
I. N. Mezhevoi ◽  
G. N. Tarasova
Author(s):  
Elena Yu. Tyunina ◽  
Valentin G. Badelin ◽  
Valentina S. Egorkina

Thermodynamic and physicochemical properties of multicomponent aqueous solutions containing biologically active solutes are important in various areas of applied chemistry and are essential for understanding the chemistry of biological systems. Interactions between nicotinic acid (NA) and L-phenylalanine (Phe) were studied in aqueous phosphate buffer solutions (pH=7.35) by differential scanning calorimetry and volume methods. Heat capacities and densities of nicotinic acid-buffer, L-phenylalanine-buffer, and nicotinic acid-L-phenylalanine-buffer mixtures were determined at T=(288.15, 298.15, 308.15 and 318.15) K using the microdifferential scanning calorimeter SCAL-1 (Pushchino, Russia) and the density meter DSA 5000 M (Anton Paar). The apparent molar heat capacities (fCp) and apparent molar volumes (Vφ,NA) of nicotinic acid in buffer solution and in buffer 0.0120 mol×kg-1 amino acid solutions were evaluated. The concentration of NA was varied from (0.0079 to 0.036) mol×kg-1. The first and second differentials values were determined for NA in an aqueous buffer solution and for NA in an aqueous amino acid buffer solution. The interaction of NA with Phe is accompanied by complex formation. NA molecules in an aqueous buffer solution are water structure breakers, then the structure breaking effects of NA decrease as a result of interactions with Phe molecules during the complex formation in an aqueous amino acid buffer solution. The results were discussed in terms of various interactions taking place in this system.Forcitation:Tyunina E.Yu., Badelin V.G., Egorkina V.S. Interaction of nicotinic acid with L-phenylalanine in buffer solutions: heat capacity and volume properties study. Izv. Vyssh. Uchebn. Zaved. Khim. Khim. Tekhnol. 2017. V. 60. N 4. P. 33-39. 


2021 ◽  
Vol 81 ◽  
pp. 153343
Author(s):  
Saki Horie ◽  
Hikaru Fujita ◽  
Rina Yamashita ◽  
Munetaka Kunishima

1963 ◽  
Vol 41 (2) ◽  
pp. 389-395 ◽  
Author(s):  
R. W. Burley

The absorption of chloroform by α- and β-lipovitellin from chloroform-saturated aqueous buffer solutions has been measured quantitatively. Absorption is rapid and reaches equilibrium values of 13 and 22% of the dry weights of α- and β-lipovitellin respectively. Ultracentrifugal examination of these lipovitellin solutions shows that chloroform absorption produces a heavier fraction that is not homogeneous and probably consists of aggregates. There appears to be a threshold concentration of chloroform in the aqueous solutions below which none is absorbed by the lipovitellins. Similar, but less extensive, experiments with the low-density lipoprotein of yolk and yolk lecithin have shown that they also absorb chloroform under the same conditions.


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