Automated Flow Injection Gradient Technique for Binding Studies of Micromolecules to Proteins Using Potentiometric Sensors:  Application to Bovine Serum Albumin with Anilinonaphthalenesulfonate Probe and Drugs

1999 ◽  
Vol 71 (13) ◽  
pp. 2541-2550 ◽  
Author(s):  
Maria E. Georgiou ◽  
Constantinos A. Georgiou ◽  
Michael A. Koupparis
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Flow Injection ◽  
Bovine Serum ◽  
Potentiometric Sensors ◽  
Binding Studies ◽  
Gradient Technique

Studies on the Interaction between Imidacloprid and Bovine Serum Albumin by Spectrometry

2013 ◽  
Vol 726-731 ◽  
pp. 199-203
Author(s):  
Rui Xin Guo ◽  
Zhi Liang Wang ◽  
Zhi Jun Hu ◽  
Guo Ling Li ◽  
Jian Qiu Chen
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Fluorescence Spectrum ◽  
Bovine Serum ◽  
Synchronous Fluorescence ◽  
Binding Studies ◽  
Single Class ◽  
Physiological Conditions ◽  
Synchronous Fluorescence Spectrometry ◽  
Hoff Equation

The binding studies of imidacloprid to bovine serum albumin (BSA) were investigated by UV-Vis absorption spectrum, fluorescence spectrum and synchronous fluorescence spectrometry. Under the simulative physiological conditions, fluorescence data revealed the presence of a single class of binding site on BSA and the dynamic quenching constants () were 6.851×104 L.mol-1 and 5.813×104 L.mol-1 at 310 and 315 K, respectively, proving the mode of action of imidacloprid with BSA as a static quenching. In addition, according to the Vant Hoff equation, ΔGθ <0 showed="" the="" combination="" of="" imidacloprid="" and="" bsa="" was="" a="" spontaneous="" process="" h="" sup="">θ <0 and="" s="" sup="">θ> 0, indicated an electrostatic interaction process. At the same time, synchronous fluorescence spectrum of BSA could tell us whether the conformation of BSA was changed by imidacloprid.

Molecularly imprinted polymeric microspheres for determination of bovine serum albumin based on flow injection chemiluminescence sensor

2010 ◽  
Vol 26 (2) ◽  
pp. 632-637 ◽  
Author(s):  
Jinghua Yu ◽  
Fuwei Wan ◽  
Congcong Zhang ◽  
Mei Yan ◽  
Xiaona Zhang ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Flow Injection ◽  
Bovine Serum ◽  
Polymeric Microspheres ◽  
Molecularly Imprinted ◽  
Flow Injection Chemiluminescence

Radioimmunoassay for pantothenic acid in blood and other tissues.

1979 ◽  
Vol 25 (1) ◽  
pp. 108-111 ◽  
Author(s):  
B W Wyse ◽  
C Wittwer ◽  
R G Hansen
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Lactobacillus Plantarum ◽  
Bovine Serum ◽  
Liquid Scintillation ◽  
Scintillation Counter ◽  
Pantothenic Acid ◽  
Biological Tissues ◽  
Binding Studies ◽  
Tissue Extracts

Abstract We describe a radioimmunoassay for pantothenic acid in biological tissues. D-Pantothenic acid was conjugated with bovine serum albumin by use of a bromoacetyl derivative of pantothenic acid, and antibody to this antigen was raised by injecting it into the foot pads of rabbits. For the radioimmunoassay, a 100-fold dilution of the resulting antiserum was incubated with radiolabeled pantothentic acid. The antibodies were precipitated and dissolved, and the radioactivity of the solution was measured in a liquid scintillation counter. Between 5 and 125 ng of pantothenic acid can be detected in 75 muL of tissue extract. Validation included recovery and precision studies, parallelism with tissue extracts, and competitive binding studies. Results of the radioimmunoassay and those of microbiological assay with use of Lactobacillus plantarum correlated well (r = 0.80).

Binding Studies of a Schiff Base Compound Containing a 1,2,4-Triazole Ring with Bovine Serum Albumin Using Spectroscopic Methods

2010 ◽  
Vol 28 (10) ◽  
pp. 1915-1922 ◽  
Author(s):  
Ping Mei ◽  
Yang Liu ◽  
Yezhong Zhang ◽  
Jiaxin Fu ◽  
Xiaohong Sun ◽  
...  
Keyword(s):  
Schiff Base ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Triazole Ring ◽  
Spectroscopic Methods ◽  
Binding Studies ◽  
Schiff Base Compound ◽  
Base Compound

Synthesis, crystal structure and bovine serum albumin–binding studies of a new Cd(II) complex incorporating 2,2′-(propane-1,3-diyl)bis(1H-imidazole-4,5-dicarboxylate)

2019 ◽  
Vol 44 (3-4) ◽  
pp. 198-205 ◽  
Author(s):  
Xiao-Fei Li ◽  
Li-Gang Ma ◽  
Yan-Qiu Yang ◽  
Yan-Ju Liu ◽  
Xiang-Ru Meng ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Three Dimensional ◽  
Entropy Change ◽  
Chain Structure ◽  
Binding Studies ◽  
Carboxylate Oxygen ◽  
Fluorescence Measurements ◽  
Bovine Serum Albumin Binding

A new Cd(II) complex, [Cd(H4pbidc)(H2O)] n (1), incorporating 2,2′-(propane-1,3-diyl)bis(1H- imidazole-4,5-dicarboxylic acid) (H6pbidc) was synthesized and characterized by elemental analysis, infrared spectra and X-ray single-crystal diffraction. In complex 1, each Cd(II) ion is hepta-coordinated, showing a significantly distorted pentagonal-bipyramidal coordination environment. Adjacent Cd(II) ions are alternately joined through two carboxylate oxygen atoms and two bridging water molecules resulting in a one-dimensional chain structure. In the solid state, adjacent chains are further linked by hydrogen bonds, forming a three-dimensional supramolecular architecture. Meanwhile, the interactions of complex 1 with bovine serum albumin were analysed by fluorescence measurements under physiological conditions. The results indicated that the fluorescence intensity of bovine serum albumin was decreased considerably upon the addition of complex 1 through a static quenching mechanism with formation of one binding site. The negative values of the thermodynamic parameters including enthalpy change (Δ H), entropy change (Δ S) and Gibbs free energy change (Δ G) showed that hydrogen bonding and van der Waals forces were the main interactions in the binding of complex 1 to bovine serum albumin, and the binding process is spontaneous in thermodynamics.

Binding studies of caffeine and theophylline to bovine serum albumin: Calorimetric and spectroscopic approach

2016 ◽  
Vol 223 ◽  
pp. 1048-1055 ◽  
Author(s):  
Tarlok S. Banipal ◽  
Navalpreet Kaur ◽  
Parampaul K. Banipal
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Studies

Determination of tannic acid after precipitation with bovine serum albumin by visible light scattering in a flow injection system

2010 ◽  
Vol 169 (1-2) ◽  
pp. 117-122 ◽  
Author(s):  
Tzong-Jih Cheng ◽  
Hsien-Yi Hsiao ◽  
Chien-Yu Chung ◽  
Po-Chung Chen ◽  
Richie L. C. Chen
Keyword(s):  
Light Scattering ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Visible Light ◽  
Tannic Acid ◽  
Flow Injection ◽  
Bovine Serum ◽  
Injection System ◽  
Flow Injection System

Equilibrium binding studies of the 1,8-dihydroxy-9,10-anthraquinone-bovine serum albumin interaction

1989 ◽  
Vol 55 (2-3) ◽  
pp. 221-227
Author(s):  
Dale Eric Wurster ◽  
Sathyanarayana M. Upadrashta
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Studies ◽  
Equilibrium Binding

On-Line Flow-Injection Chemiluminescence Determination of Bovine Serum Albumin Using Surfactant-Enhanced Dichlorofluorescein-Hypochlorite System

2010 ◽  
Vol 43 (14) ◽  
pp. 2275-2282 ◽  
Author(s):  
Chun-Bao Huang ◽  
Kai Zhang ◽  
Wen-Yue Yang ◽  
Sheng-Fu Wang
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Flow Injection ◽  
Bovine Serum ◽  
Line Flow ◽  
On Line ◽  
Flow Injection Chemiluminescence
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