scholarly journals Binding of 2-(4'-hydorxyphenylazo)benzoic acid to bovine serum albumin characterized by optical spectroscopy and equilibrium dialysis.

1981 ◽  
Vol 4 (1) ◽  
pp. 65-68 ◽  
Author(s):  
TAMIKO SAKURAI ◽  
SEISHI TSUCHIYA ◽  
HIDEO MATSUMARU
Keyword(s):  
Bovine Serum Albumin ◽  
Benzoic Acid ◽  
Serum Albumin ◽  
Optical Spectroscopy ◽  
Bovine Serum ◽  
Equilibrium Dialysis

Screening radioimmunoassay for aldosterone in preheated plasma without extraction and chromatography.

1980 ◽  
Vol 26 (1) ◽  
pp. 41-45
Author(s):  
T M Connolly ◽  
L Tibor ◽  
K H Gless ◽  
P Vecsei
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Proteins ◽  
Equilibrium Dialysis ◽  
Screening Method ◽  
Plasma Aldosterone ◽  
Plasma Samples ◽  
Bovine Serum Albumin Conjugate ◽  
Native Plasma

Abstract We directly estimated plasma aldosterone radioimmunologically with use of an antiserum raised against an aldosterone-3-oxime/bovine serum albumin conjugate, the estimation being on samples with and without heating (60 degrees C), and diluted and undiluted. Values so obtained were compared with those by radioimmunoassay after extraction and chromatography. The correlation--even negative values were obtained--was poorest when the steroid was directly estimated in nonheated, undiluted plasma. Correlations were best (r = 0.918) for preheated and diluted native plasma, and the interassay CV was 9.8% (n = 57). However, there were some extraordinarily high values. After equilibrium dialysis of native and preheated (60 degrees C) plasma (15 plasma samples), the percentages of apparent free aldosterone and cortisol increased from 51.4 +/- 2.6% (SEM) to 64.3 +/- 1.6% and from 11.5 +/- 2.2% to 61.1 +/- 1%, respectively. We conclude that aldosterone-binding proteins play a role in direct radioimmunoassays of aldosterone in plasma, but by heating (with or without diluting) the plasma, direct assay can be used as a simple, fast, and inexpensive screening method.

scholarly journals Effect of arsenic on paracetamol binding to bovine serum albumin using site specific probes

2012 ◽  
Vol 1 (11) ◽  
pp. 361-365 ◽  
Author(s):  
Riaz Uddin ◽  
Nadia Saffoon ◽  
Md. Ashraful Alam
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Equilibrium Dialysis ◽  
Pharmaceutical Journal ◽  
Specific Probe ◽  
Free Concentration ◽  
Site Specific ◽  
Warfarin Sodium ◽  
High Affinity Binding Site

Arsenic contamination in groundwater is a global health challenge. A large number of people worldwide are affected by arsenic poisoning. Paracetamol is a widely used analgesic-antipyretic drug. Effect of arsenic on paracetamol binding to protein has been investigated using two site specific probes and equilibrium dialysis method was used for the experiment. In absence of any site specific probes free concentration of paracetamol bound to bovine serum albumin increased from 3.95 ± 1.164% to 25.36 ± 1.164%. In presence of site-I specific probe warfarin sodium the % release of drug was steady at around 14%. But in presence of site-II specific probe an increment of free drug concentration was observed from 14.38 ± 1.164% to 54.72 ± 1.552%. Thus it can be assumed that the free concentration of paracetamol was increased to a greater extent in presence of arsenic and probably arsenic bound to site-II of BSA. Thus arsenic may displace paracetamol by binding with high affinity binding site, site-II in the BSA and probably arsenic has little effect to site-I.DOI: http://dx.doi.org/10.3329/icpj.v1i11.12061 International Current Pharmaceutical Journal 2012, 1(11): 361-365 

Interaction of theophylline with bovine serum albumin and competitive displacement by benzoic acid.

1985 ◽  
Vol 33 (7) ◽  
pp. 2648-2653 ◽  
Author(s):  
JUZIRO NISHIJO ◽  
NORIKO MORITA ◽  
SHOZO ASADA ◽  
HIROKO NAKAE ◽  
EMIKO IWAMOTO
Keyword(s):  
Bovine Serum Albumin ◽  
Benzoic Acid ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Competitive Displacement

scholarly journals Binding Aspects of 2-(4-Hydroxyphenylazo)benzoic Acid to Bovine Serum Albumin in the Limited Mixing Ratio

1988 ◽  
Vol 61 (8) ◽  
pp. 2727-2730
Author(s):  
Kunio Takeda ◽  
Katsushi Sasa ◽  
Kazuaki Hachiya ◽  
Mamoru Murata ◽  
Koichiro Aoki
Keyword(s):  
Bovine Serum Albumin ◽  
Benzoic Acid ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Mixing Ratio

Mechanism of the binding of 2-(4′-hydroxyphenylazo)benzoic acid to bovine serum albumin

1985 ◽  
Vol 21 (2) ◽  
pp. 127-136 ◽  
Author(s):  
Kiyofumi Murakami ◽  
Takayuki Sano ◽  
Shiro Tsuchie ◽  
Tatsuya Yasunaga
Keyword(s):  
Bovine Serum Albumin ◽  
Benzoic Acid ◽  
Serum Albumin ◽  
Bovine Serum

scholarly journals Binding of branched-chain 2-oxo acids to bovine serum albumin

1982 ◽  
Vol 204 (1) ◽  
pp. 265-272 ◽  
Author(s):  
G Livesey ◽  
P Lund
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Plasma ◽  
Bovine Serum ◽  
Equilibrium Dialysis ◽  
Rat Plasma ◽  
Gel Chromatography ◽  
High Concentration ◽  
Branched Chain ◽  
Inhibition Studies

1. Binding of branched-chain 2-oxo acids to defatted bovine serum albumin was shown by gel chromatography and equilibrium dialysis. 2. Equilibrium-dialysis data suggest a two-side model for binding in Krebs-Henseleit saline at 37 degrees C with n1 = 1 and n2 = 5. Site association constants were: 4-methyl-2-oxovalerate, k1 = 8.7 × 10(3) M-1, k2 = 0.09 × 10(3) M-1; 3-methyl-2-oxovalerate, k1 = 9.8 × 10(3) M-1, k2 = 0.08 × 10(3) M-1; 3-methyl-2-oxobutyrate, k1 = 1.27 × 10(3) M-1, k2 = less than 0.05 × 10(3) M-1. 3. Binding of 4-methyl-2-oxovalerate to defatted albumin in a phosphate-buffered saline, pH 7.4, gave the following thermodynamic parameters: primary site delta H0(1) = -28.6kJ . mol-1 and delta S0(1) = -15.2J . mol-1 . K-1 (delta G0(1) = -24.0kJ . mol-1 at 37 degrees C) and secondary sites delta H0(2) = -25.4kJ . mol-1 and delta S0(2) = -46.1J . mol-1 . K-1 (delta G0(1) = -11.2kJ . mol-1 at 37 degrees C). Thus binding at both sites is temperature-dependent and increases with decreasing temperature. 4. Inhibition studies suggest that 4-methyl-2-oxovalerate may associate with defatted albumin at a binding site for medium-chain fatty acids. 5. Binding of the 2-oxo acids in bovine, rat and human plasma follows a similar pattern to binding to defatted albumin. The proportion bound in bovine and human plasma is much higher than in rat plasma. 6. Binding to plasma protein, and not active transport, explains the high concentration of branched-chain 2-oxo acids leaving rat skeletal muscle relative to the concentration within the tissue, but does not explain the 2-oxo acid concentration gradient between plasma and liver.

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