scholarly journals The Hematin-Binding Reaction as a Basis for Serum Albumin Determination

1952 ◽  
Vol 199 (2) ◽  
pp. 911-921
Author(s):  
Morris Rosenfeld ◽  
Douglas M. Surgenor
Keyword(s):  
Serum Albumin ◽  
Binding Reaction

Study on Binding Reaction between Flucytosine and Bovine Serum Albumin

2005 ◽  
Vol 23 (9) ◽  
pp. 1151-1156 ◽  
Author(s):  
Cheng-Nong Yan ◽  
Hua-Xin Zhang ◽  
Ping Mei ◽  
Yi Liu
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Reaction

scholarly journals Voltammetric albumin quantification based on its interaction with carminic acid

2006 ◽  
Vol 71 (4) ◽  
pp. 385-396 ◽  
Author(s):  
Wei Sun ◽  
Yunying Han ◽  
Kui Jiao
Keyword(s):  
Serum Albumin ◽  
Human Serum ◽  
Mercury Electrode ◽  
Carminic Acid ◽  
Optimal Conditions ◽  
Binding Reaction ◽  
Peak Current ◽  
Dropping Mercury Electrode ◽  
Voltammetric Detection

In a weak acidic Britton-Robinson (B-R) buffer of pH 4.0, human serum albumin (HSA) can react rapidly with carminic acid (CAA) to form a supramolecular complex. Microelectrostatic fields in the molecular structure of HSA cause the electrostatic binding reaction of the positively charged CAA with the negatively charged HSA. CAA has a sensitive, second order derivative linear sweep voltammetric reductive peak at - 0.54 V (vs. SCE) on a dropping mercury electrode (DME). After the addition of HSA to a CAA solution, the reductive peak current of CAA decreased without a shift of the peak potential. Based on the decrease of the peak current, a sensitive voltammetric method for the determination of microamounts of the protein is proposed. The conditions for the binding reaction and the voltammetric detection were optimized. Under the optimal conditions, the decrease of the voltammetric detection were optimized. Under the optimal conditions, the decrease of the voltammetric peak current was in proportion to the quantity of HSA in the range of 2.0 to 70.0 mg l-1, with a linear regression equation ?Ip"(nA)=11.74 C (mg l-1)-12.33 and a detection limit of 2.0 mg l-1 (3?). The method was further applied to the detection of different kinds of proteins, such as bovine serum albumin (BSA), oval albunim (OVA), lipase, etc. The established method was further applied to the determination of the albumin content in human serum samples and the results obtained by this method were in good agreement with the traditional Coomassie Brilliant Blue G-250 (CBB G-250) spectrophotometric method. The binding mechanism is discussed and the binding ratio was calculated from the voltammetric data.

Antimicrobial Activity and Interaction with Bovine Serum Albumin of Nickel(II) Complex

2012 ◽  
Vol 554-556 ◽  
pp. 1831-1834
Author(s):  
Yu Fen Liu ◽  
Hai Tao Xia ◽  
De Fu Rong
Keyword(s):  
Escherichia Coli ◽  
Antimicrobial Activity ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Ground State ◽  
Bovine Serum ◽  
Binding Constants ◽  
Quenching Mechanism ◽  
Binding Reaction ◽  
Physiological Conditions

The binding reaction of nickel(II) complex [Ni(C16H20N2)2•(H2O)2]Cl2•C3H7NO with bovine serum albumin(BSA) was studied by fluorescence spectroscopy under the simulative physiological conditions. The experimental results show that the fluorescence quenching of BSA by nickel(II) complex is a result of the formation of ground state complex and the quenching mechanism was static quenching. The binding constants were 4.24×103L•mol−1at 293K with one binding site. The antimicrobial activity study found that the nickel(II) complex was active against Escherichia coli, Staphylococcus aureus and Bacillus subtilis.

scholarly journals The Basic Study on the Binding Reaction between Bovine Serum Albumin and Methamphetamine.

Eisei kagaku ◽  
1995 ◽  
Vol 41 (2) ◽  
pp. 163-166 ◽  
Author(s):  
YUKO YANAGISAWA ◽  
KENICHI NAKAZATO ◽  
TATSUO NAGAI
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Basic Study ◽  
Binding Reaction

scholarly journals Investigation on the Competition Interaction of Synthetic Food Colorants and Ciprofloxacin Hydrochloride with Bovine Serum Albumin by Fluorescence Spectroscopy

2011 ◽  
Vol 2011 ◽  
pp. 1-7 ◽  
Author(s):  
Baosheng Liu ◽  
Chao Yang ◽  
Jing Wang ◽  
Chunli Xue ◽  
Yunkai Lü
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Sunset Yellow ◽  
Food Colorants ◽  
Binding Reaction ◽  
Ciprofloxacin Hydrochloride ◽  
Synthetic Food Colorants ◽  
Binding Distance

The effects of synthetic food colorants like tartrazine (TTZ), sunset yellow (SY), and erythrosine (ETS) on the binding reaction between ciprofloxacin hydrochloride (CPFX) and bovine serum albumin (BSA) were investigated by fluorescence spectroscopy in the aqueous solution of pH = 7.40. Results showed that CPFX caused the fluorescence quenching of BSA through a static quenching procedure and the primary binding site was located at subdomain IIA of BSA (site I). According to the calculated thermodynamic parameters, it confirmed that CPFX bound to BSA by electrostatic interaction. In addition, the colorants affected the formation of BSA-CPFX complex. This resulted in an increase of the free, biological active fraction of CPFX. The binding distance of BSA-CPFX systems was evaluated according to Förster's theory. Results suggested that the binding distance were increased in the presence of synthetic food colorants.

Study of the Interaction between Zinc Complex and Bovine Serum Albumin by Fluorescence Spectroscopy

2012 ◽  
Vol 554-556 ◽  
pp. 1678-1681 ◽  
Author(s):  
Yu Fen Liu ◽  
Hai Tao Xia ◽  
De Fu Rong
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Binding Sites ◽  
Bovine Serum ◽  
Binding Constants ◽  
Gibbs Free Energy Change ◽  
Binding Reaction ◽  
Physiological Conditions ◽  
Number Of Binding Sites

The binding reaction of Zn(II) complex [Zn(C8H10N)2Cl2] with bovine serum albumin(BSA) was studied by fluorescence spectroscopy under the simulative physiological conditions. The intrinsic fluorescence of BSA could be quenched by Zn(II) complex. The quenching mechanism was suggested as static quenching according to the Stern–Volmer equation. The binding constants Kband the number of binding sites n were calculated. The Zn(II) complex exhibit good binding propensity to bovine serum albumin having relatively high binding constant values. The thermodynamic parameters indicate that the hydrogen bonds and van der Waals forces play a major role in BSA-Zn(II) complex association. The process of binding was spontaneous, in which Gibbs free energy change (ΔG) was negative.

Improvement of an artificial test substrate technique for evaluation of em immunocytochemical labeling

1987 ◽  
Vol 45 ◽  
pp. 762-763
Author(s):  
G. D. Gagne ◽  
M. F. Miller
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Artificial Substrate ◽  
Chemical Fixation ◽  
As If

We recently described an artificial substrate system which could be used to optimize labeling parameters in EM immunocytochemistry (ICC). The system utilizes blocks of glutaraldehyde polymerized bovine serum albumin (BSA) into which an antigen is incorporated by a soaking procedure. The resulting antigen impregnated blocks can then be fixed and embedded as if they are pieces of tissue and the effects of fixation, embedding and other parameters on the ability of incorporated antigen to be immunocyto-chemically labeled can then be assessed. In developing this system further, we discovered that the BSA substrate can also be dried and then sectioned for immunolabeling with or without prior chemical fixation and without exposing the antigen to embedding reagents. The effects of fixation and embedding protocols can thus be evaluated separately.

Sign in / Sign up

Export Citation Format

Share Document