• Archives of Pharmacal Research
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• v.12 no.3
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• pp.160-165
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• 1989

Binding of sulfaethidole to bovine serum albumin was studied by equilibrium dialysis, fluorescence probe technique, uv difference spectrophotometry and circular dichroism. Equilibrium dialysis method enabled us to estimate the total number of drug binding sites of albumin molecule. For sulfaethidole, albumin had 6 primary and 40 secondary binding sites. The primary and secondary binding constants were 0.9 * 10/sup 5/ M/sup -1/ and 0.2 * 10/sup 6/ M/sup -1/, respectivitely. 1-Anilino-8-naphthalenesulfonate (ANS) and 2-(4-hydroxylbenzeneazo)- benzoic acid (HBAB) were used as the fluorescence probe and the uv spectrophotometric probe, respectively. In fluorescence probe technique, results indicated that the number of higher affinity drug binding site of albumin was 1 and the number of lower affinity drug binding sites of albumin was 3, and the primary and secondary drug binding constants for bovine serum albumin were 2.15 * 10/sup 5/M/sup -1/ and 1.04 * 10/sup 5/ M/sup -1/, respectively. In uv difference spectrophotometry, binding sites were 3 and binding constant was 1.88 * 10/sup 5/M/sup -1/. The above spectrophotometry, binding sites were 3 and binding constant was 1.88 * 10/sup 5/M/sup -1/. The above results suggest that several different methods should be used in ompensation for insufficient information about drug binding to albumin molecule given by only one method.

• YAKHAK HOEJI
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• v.33 no.6
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• pp.345-349
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• 1989

This paper was attempted to investigate effect of angiotensin inhibitor (loading dose 25, 50, $100{\mu}g/kg$ and maintenance dose 12.5, 25, $50{\mu}g/kg/hr$) on the pharmacokinetics of furosemide (5 mg/kg i.v) in rabbit. The plasma concentrations of furosemide increased by angiotensin inhibitor and the relative bioavailability of furosemide increased from 118.1% to 193.2% by the inhibitor. The protein binding of furosemide decreased by angiotensin inhibitor in bovine serum albumin ($2.17\;{\times}\;10^{-4}M$) by equilibrium dialysis method. Consequently, dosage regimen of furosemide might be adjusted carefully when furosemide is administered with angiotensin inhibitor.

• Journal of Pharmaceutical Investigation
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• v.19 no.1
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• pp.15-20
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• 1989

The displacement of protein bound sulfonamides (sulfisoxazole, sulfamethoxazole, sulfisomidine) by furosemide was investigated in bovine serum albumin by equilibrium dialysis method. Furosemide $(2{\times}10^{-4}M)$ in bovine serum albumin ($7.24{\times}10^{-5}$, $1.45{\times}10^{-4}$, $2.89{\times}10^{-4}M$). Sulfisoxa캐1e and furosemide were bound reversibly to bovine serum albumin and competitive for the same binding sites when administered together. Consequently, dosage regimen of sulfisoxazole should be adjusted carefully when sulfisoxazole is administered along with furosemide.

• Journal of Pharmaceutical Investigation
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• v.4 no.1_2
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• pp.25-30
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• 1974

The adsorption of nalidixic acid on human erythrocytes was found to expressed by Freundlich's isotherm. The amount of adsorption of nalidixic acid on erythrocytes increased with an increase of pH. The adsorption of nalidixic acid on human plasma was found to expressed at Scatchard's equation by the equilibrium dialysis method. An influence of pH on adsorption of nalidixic acid to human plasma proteins was studies at pH 4-10. It was found that the degree of adsorption increase with the increase of pH from 4-6, but descreased above pH 9.

• Journal of Pharmaceutical Investigation
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• v.6 no.1
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• pp.14-17
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• 1976

Binding of nalidixic acid with plasma of male and female rats, dogs, and rabbits was studied in vitro using the method of equilibrium dialysis in 1/15 mole phosphate buffer (pH 7.4). Rat plasma had the most extensive binding capacity followed by dog and rabbit plasma, and the plasma of female had more extensive capability than male in rat and rabbit but it was reversed in dog.

• Journal of The Korean Society of Clinical Toxicology
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• v.1 no.1
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• pp.6-11
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• 2003

Various forms of dialytic techniques are available for detoxification. Hemodialysis, hemoperfusion and hemofiltration (hemodialfiltration) are the main treatment modalities. Because these modalities are rather invasive and expensive, it must be decided in balance of the risk and benefit to the patient. The prime consideration in the decision is based on the clinical features of poisoning; hemodialysis or hemoperfusion should be considered in general if the patient's condition progressively deteriorates despite intensive supportive therapy. The hemodialysis technique relies on passage of the toxic agent through a semipermeable membrane so that it can equilibrate with the dialysate and subsequently removed. It needs a blood pump to pass blood next to a dialysis membrane, which allows agents permeable to the membrane to pass through and reach equilibrium. Solute (or drug) removal by dialysis has numerous determinants such as solute size, its lipid solubility, the degree to which it is protein bound, its volume of distribution etc. The technique of hemoperfusion is similar to hemodialysis except there is no dialysis membrane or dialysate involved in the procedure. The patient's blood is pumped through a perfusion cartridge, where it is in direct contact with adsorptive material (usually activated charcoal) that has a coating material such as cellulose. This method can be used successfully with lipid-soluble compounds and with higher-molecular-weight compounds than for hemodialysis. Protein binding does not significantly interfere with removal by hemoperfusion. In conclusion, hemodialysis, hemoperfusion and hemofiltration can be used effectively as adjuncts to the management of severely intoxicated patients.

• Bulletin of the Korean Chemical Society
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• v.25 no.6
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• pp.791-795
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• 2004

The binding of cethyl trimethylammonium bromide, (CTAB) with human serum albumin (HSA) has been investigated at 5 mM phosphate buffer pH 7.0, 27 $^{\circ}C$ and various ionic strength using ion selective membrane electrodes. This method is faster and much more accurate than equilibrium dialysis technique, so provides sufficient and accurate data for binding data analysis. A novel and simple method was introduced for resolution and characterization of binding sets on basis of binding capacity concept. The values of Hill binding parameters were estimated for each set and used for calculation of intrinsic binding affinity. The results interpreted on basis of nature of forces which interfered in the interaction and represent the existence of three and two binding sets for binding of CTAB at $10^{-4}$ and $10^{-3}$ M of NaBr, respectively.

• Archives of Pharmacal Research
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• v.27 no.9
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• pp.978-983
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• 2004

The effects of glycyrrhizic acid (GLZ) on protein binding of diltiazem, verapamil, and nifedipine were investigated. Protein binding studies (human serum, human serum albumin (HSA) and (X1-acid glycoprotein (AAG)) were conducted using the equilibrium dialysis method with and without addition of GLZ. The binding parameters, such as the number of moles of bound drug per mole of protein, the number of binding sites per protein molecule, and the association con-stant, were estimated using the Scatchard plot. The serum binding of nifedipine, verapamil, and diltiazem was displaced with addition of GLZ, and the decreases of Ks for serum were observed. GLZ decreased the association constants of three drugs for HSA and AAG, while the binding capacity remained similar with addition of GLZ. Although the characteristics of interaction were not clear, GLZ seemed to mainly affect HSA binding of nifedipine rather than AAG binding, while GLZ seemed to affect both AAG- and HSA-bindings of verapamil and dilt-iazem resulting in a serum binding displacement.

• Bulletin of the Korean Chemical Society
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• v.23 no.8
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• pp.1073-1077
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• 2002

Binding of dodecyl trimethylammonium bromide (DTAB) to human and bovine hemoglobin and globin samples has been investigated in 50 mM glycine buffer pH = 10, I = 0.0318 and 300 K by equilibrium dialysis and temperature scanning spectrophotometry techniques and method for calculation of average hydrophobicity. The binding data has been analyzed, in terms of binding capacity concept $({\theta})$, Hill coefficient (nH) and intrinsic Gibbs free energy of binding $({\Delta}Gbv).$ The results of binding data, melting point (Tm) and average hydrophobicity show that human hemoglobin has more structural stability than bovine hemoglobin sample. Moreover the results of binding data analysis represent the systems with two and one sets of binding sites for hemoglobin and globin, respectively. It seems that the destabilization of hemoglobin structure due to removal of heme group, is responsible of such behavior. The results indicating the removal of heme group from hemoglobin caused the depletion of first binding set as an electrostatic site upon interaction with DTAB and exposing the hydrophobic patches for protein.

• Journal of radiological science and technology
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• v.11 no.1
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• pp.25-31
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• 1988

Studies on the clinical significance with Amerlex $FT_{4}$ RIA kit observing the determination of $FT_{4}$ were investigated using a tracer as $^{125}I-T_{4}$ derivative which is not almostly bound to thyroxine binding globulin, etc. The results are followed; 1. $FT_{4}$ value($1,55{\pm}0.38ng/100ml$) of normal group was not accorded that of hyperthyroidism with Amerlex $FT_{4}$ RIA kit, and was higher than that of hypothyroidism. 2. $FT_{4}$ value was lower level in chronic-kidney disfunction syndrome whereas, it was normal in a cancer patient, a woman in pregnancy and a patient in TBG disfunction. 3. The value of this method is a good corelationship at that of equilibrium dialysis method. (r=0.931) 4. $FT_{4}$ value by this kit was linear relationship to those of the other kit (Gamma Coat and Liquisol), and the normal value of each methods was also similar. As mentioned above, this method is more simple and rapid, compared to the other method. Therefore, it was thought that this method is a very useful clinically.