The Binding Constant of Estradiol to Bovine Serum Albumin. An Upper-Level Experiment Utilizing Tritium-Labeled Estradiol and Liquid Scintillation Counting

2006 ◽  
Vol 83 (2) ◽  
pp. 294 ◽  
Author(s):  
Peihong Liang ◽  
Bhavin Adhyaru ◽  
Wright L. Pearson ◽  
Kathryn R. Williams
1979 ◽  
Vol 25 (1) ◽  
pp. 108-111 ◽  
Author(s):  
B W Wyse ◽  
C Wittwer ◽  
R G Hansen

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).


2011 ◽  
Vol 347-353 ◽  
pp. 1281-1286
Author(s):  
Shan Shan Huang ◽  
Feng Zuo Qu ◽  
Tong Kuan Xu ◽  
Li Cui

The interaction conditions between the water-soluble chitosans(WSC) and bovine serum albumin (BSA) was studied by Ultraviolet-visible absorption and fluorescence spectrometries. It was shown there was a good linear relationship between the absorbency A and the BSA concentration(0~1.5g/L) and WSC concentration (0~1.5 g/L). The fluorescence quenching of WSC to BSA was static quenching. When the temperature is 30°C, its binding constant Ka=5.35×104 L/mol, binding site n=1.05. The influence of WSC on the conformation of BSA was analyzed by sychronous fluorescence spectra and three-dimensional fluorescence spectrum.


2004 ◽  
Vol 40 (4) ◽  
pp. 3027-3029 ◽  
Author(s):  
P.P. Macaroff ◽  
D.M. Oliveira ◽  
Z.G.M. Lacava ◽  
R.B. Azevedo ◽  
E.C.D. Lima ◽  
...  

2014 ◽  
Vol 664 ◽  
pp. 402-409
Author(s):  
Qing Ming Wang ◽  
Jia Liu ◽  
Tian Xing Zhang ◽  
Feng Zhu ◽  
Xin Hui Tang

We investigated the mutual interaction of daidzin with bovine serum albumin (BSA) by fluorescence spectroscopy. The results revealed that daidzin cause the fluorescence quenching of BSA through a static quenching procedure. The Stern-Volmer quenching constant (Ksv) were calculated at different temperature. The binding site (n), apparent binding constant (Ka) and corresponding thermodynamic parameters △Go, △Ho, △Sowere calculated and the van der Waals interaction, hydrogen bonds and hydrophobic interactions play an important role in stabilizing the complex. Besides, we also studied the effect of Cu2+, Ni2+, Mn2+and Co2+on the binding constants between daidzin and BSA, it is shows that the binding of BSA and daidzin is strengthened in the presence metal ions.


2020 ◽  
Vol 65 (6) ◽  
pp. 468
Author(s):  
N. A. Goncharenko ◽  
O. P. Dmytrenko ◽  
O. L. Pavlenko ◽  
M. P. Kulish ◽  
I. P. Pundyk ◽  
...  

The fluorescence (FL) quenching in aqueous solutions of doxorubicin (DOX)–bovine serum albumin (BSA)–gold nanoparticles (AuNPs) is studied. The existence of additional mechanisms of DOX-BSA complex formation leading to an increase in the binding constant K and a decrease in the number of binding sites n and the distance between the fluorophore and energy acceptors due to the presence of gold nanoparticles is shown.


2007 ◽  
Vol 11 (02) ◽  
pp. 109-117 ◽  
Author(s):  
Samson Khene ◽  
Abimbola Ogunsipe ◽  
Edith Antunes ◽  
Tebello Nyokong

This work reports on the microwave synthesis of tetrasulfonated tin phthalocyanine and tetrasulfonated tin α,β,γ-tetrabenzcorrole. The latter was only formed at low ratios (<1:8) of 4-sulfophthalic acid to urea. Both complexes are aggregated in aqueous media, but can be partly or fully disaggregated by the addition of Triton X-100. The α,β,γ-tetrabenzcorrole complex has lower triplet life times and yields, while the binding constant and quenching (of bovine serum albumin) constant are lower for α,β,γ-tetrabenzcorrole compared to tetrasulfonated tin phthalocyanine.


2006 ◽  
Vol 84 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Fei Lu ◽  
Jing-Hao Pan ◽  
Yun Liu ◽  
Hongfen Zhang ◽  
Yujing Guo ◽  
...  

A supramolecular complex of bovine serum albumin (BSA) with acid cyanine 5R (AC 5R, C.I. acid blue 113, C.I.: 26360) has been shown to form in Tris–HCl buffer solution (pH 7.42) by linear sweep voltammetry (LSV), fluorimetry, and spectrophotometry. The binding ratio and binding constant of BSA with AC 5R have been detected by LSV and fluorimetry. The binding mechanism is also preliminarily discussed. In Tris–HCl buffer solution (pH 7.42), AC 5R can easily be reduced on the mercury electrode, and it has a well-defined LSV peak current (Ip) and peak potential (Ep) at –0.65 V (vs. SCE). In the presence of BSA, the Ipof AC 5R decreases, and the peak potential (Ep) shifts to a more positive potential. The decrease of the second-order derivative of reductive peak current (ΔIp") of AC 5R is proportional to the logarithm of BSA concentration in the range of 1.54 × 10–8mol·L–1– 1.54 × 10–5mol·L–1(r = 0.9931 – 0.9977). The limit of detection of BSA is 9.0 × 10–9mol·L–1. The relative standard deviation is 1.83% (n = 10), and the standard recovery is 97.5%–104.8%. This method can be used to determine BSA concentration on the basis of the interaction of BSA with AC 5R.Key words: bovine serum albumin (BSA), acid cyanine 5R (AC 5R), supramolecule, binding ratio, binding constant, fluorimetry, spectrophotometry, electroanalytical method.


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