scholarly journals Stopped-flow Kinetic Studies of Cu2+Ion Binding to Bovine Serum Albumin

1984 ◽  
Vol 57 (10) ◽  
pp. 2712-2717 ◽  
Author(s):  
Naohisa Kure ◽  
Hitoshi Nakatsuji ◽  
Takayuki Sano ◽  
Tatsuya Yasunaga
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Kinetic Studies ◽  
Ion Binding ◽  
Stopped Flow

scholarly journals Physicochemical Peculiarities of Iodine-Dimethylsulfoxide-H2O Solutions and Effect on Ion Binding to Bovine Serum Albumin

2013 ◽  
Vol 2013 ◽  
pp. 1-5
Author(s):  
K. Grigoryan ◽  
H. Shilajyan
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Entropy Change ◽  
Ion Binding ◽  
Fluorescence Energy Transfer ◽  
Iodide Ion ◽  
Different Temperatures ◽  
Fluorescence Energy

The interaction of iodine with bovine serum albumin (BSA) in dimethylsulfoxide (DMSO) aqueous solutions was studied by means of fluorescence and UV/Vis absorption spectroscopy methods. Physicochemical peculiarities of these solutions were revealed. The results showed that the tri-iodide ion formed in the 1DMSO : 2H2O solution caused the fluorescence quenching of BSA. The modified Stern-Volmer quenching constant and corresponding thermodynamic parameters, the free energy change (), enthalpy change (), and entropy change (), at different temperatures (293, 298, and 303 K) were calculated, which indicated that the hydrophobic and electrostatic interactions were the predominant operating forces. The binding locality distance r between BSA and tri-iodide ion at different temperatures was determined based on Förster nonradiation fluorescence energy transfer theory.

Pressure Jump Studies of Proteins. I. Isomerization of Bovine Serum Albumin at Neutral pH

1971 ◽  
Vol 49 (12) ◽  
pp. 1267-1275 ◽  
Author(s):  
D. E. Goldsack ◽  
P. M. Waern
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Change ◽  
Bovine Serum ◽  
Ph Dependence ◽  
Kinetic Studies ◽  
Relaxation Effect ◽  
Pressure Jump ◽  
Relaxation Effects ◽  
Ph Range

Pressure jump kinetic studies of the conformational change occurring in bovine serum albumin in neutral solutions have been carried out over the pH range 6.5–9.5. Two distinct relaxation effects are observed at each pH. The faster relaxation is attributed to binding of the dye to the protein, and the slower relaxation is related to the conformational change occurring in the protein. This slower relaxation effect is pH dependent with a maximum value near pH 8. Detailed analysis of these data leads to a mechanism for the conformational change which indicates that the one form of the protein has an ionizable group with a pK of 8.7 which changes to a pK of 6.7 when the protein undergoes the conformational change. A simple iterative procedure is given for analyzing the pH dependence of a relaxation time constant for a cyclic mechanism involving only one ionizing group controlling the conformational change.

scholarly journals Stopped-Flow Kinetic Study of the Complex Formation between Pyridoxal 5′-Phosphate and Bovine Serum Albumin

1986 ◽  
Vol 59 (11) ◽  
pp. 3399-3403 ◽  
Author(s):  
Kiyofumi Murakami ◽  
Yukio Kubota ◽  
Yasuo Fujisaki ◽  
Takayuki Sano
Keyword(s):  
Bovine Serum Albumin ◽  
Complex Formation ◽  
Serum Albumin ◽  
Kinetic Study ◽  
Bovine Serum ◽  
Stopped Flow

Kinetic studies on binding of bovine serum albumin with 1-anilino-8-naphthalene sulfonate

FEBS Letters ◽  
1974 ◽  
Vol 43 (3) ◽  
pp. 293-296 ◽  
Author(s):  
Hiroshi Nakatani ◽  
Masafumi Haga ◽  
Keitaro Hiromi
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Kinetic Studies
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