• Archives of Pharmacal Research
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• v.7 no.2
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• pp.87-93
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• 1984

The effects of ionic strength and pH on the binding of cefazolin to bovine serum albumin (BSA) were studied by UV difference spectrophotometry. As ionic strength at constant pH and temperature increases, the apparent bining constant decreased but the number of binding sites remained almost constant at 2. The constancy of the number of binding sites with increasing the ionic strength suggests that purely electrostatic forces between BSA and drug do not have great importance in the drug binding, even though there is a decrease in the apparent binding constant. Thus, the effect of ionic strength on the interaction between drug and BSA may be explained by the changes in ionic atmosphere of the aggregated BSA molecules and competitive inhibition by phosphate ions. In addition, the higher apparent binding constant at high ionic strength is explained by conformational changes of BSA from its aggregate forms into subunits. The pH effects on the afinity of interactions indicated that the binding affinity of cefazoline is higher in the neutral region than in the alkaline region. An d at high pH value, the number of binding sites decreased from 2 to 1 because of the conformational change of BSA in the alkaline region.

• Archives of Pharmacal Research
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• v.7 no.2
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• pp.95-99
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• 1984

Binding of sulfaethidole to bovine serum albumin (BSA) was studied by circular dichroism. The effects of pH and ionic strength on the binding of sulfaethidole to BSA were investigated. It was found that one primary binding site on the BSAM was capable of inducing optical activity in the presence of sulfaethidole. Enhancement of the induced ellipticity of sulfaethidole upon addition to BSA was not much affected by the change of pH and ionic strength. Taking the effects of pH and ionic strength into consideration, it seems that the binding of sulfaethidole to BSA was not much affected by electrostatic and ionic interactions. Therefore, it might be assumed that the binding was mainly due to the hydrophobic interactions. Sulfaethidole seems to be a reasonable CD probe for the study of hydrophobic drug interactions.

• Archives of Pharmacal Research
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• v.4 no.2
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• pp.99-107
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• 1981

To investigate the protein binding characteristics of ibuprofenlysine, the effects of drub conentration, pH, ionic strength and protein concentration on the binding of drug to protein concentration on the binding of drug to protein were studied by fluorescence probe method. The conformational change of protein was investigated by circular dichroism (CD) measurement. As the concentration of drug increases, the association constant decreases. These may be due to complex formation of the probe and drug, or the interaction of the protein-probe complex and drug. The association constant for ibuprofenlysine increased with increasing protein concentration. These finding suggest a sharing of one ibuprofenlysine molecule by more than one protein molecule in the binding. The binding between ibuprofenlysine and protein was dependent on pH and ionic strength. It seems that both hydrophobic binding and some electrostatic forces are involved in the binding of ibuprofenlysing to protein.

• Journal of Pharmaceutical Investigation
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• v.19 no.3
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• pp.163-171
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• 1989

To investigate the protein binding characteristics of cephalothin, the effects of ionic strength, pH and temperature on the binding of cephalothin to bovine serum albumin (BSA) were studied by UV difference spectrophotometric method. With increasing ionic strength at constant PH and temperature, association constant decreased, but the number of binding sites sites was about 2 constantly. It may be deduced that the binding process is not only due to electrostatic forces. And the increased association constant at high ionic strength is explained by conformational changes of BSA from complex to subunits. The pH effect on the affinity of interaction indicated that the binding affinity of drug is higher in the neutral region than in the alkaline region. And, at high pH value, the number of binding sites decreased from 2 to 1 because of the conformational changes of BSA in alkaline region. The decrease in binding affinity of BSA to drug with increasing temperature was characteristic of an exothermic reaction. And the negative sign of ${\Delta}G^{\circ}$ meant that the binding process occurs spontaneously under the experimental conditions. In cephalothin-BSA complex formation, since the net enthalpy change value and entropy change value are positive, it is assumed that hydrophobic bindings are predominant in this binding process.

• YAKHAK HOEJI
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• v.26 no.2
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• pp.85-90
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• 1982

The binding of the 1-anilinonaphthalene-8-sulfonate(ANS) to bovine serum albumin was studied by fluorescence spectroscopy. The effect of pH, ionic strength, and protein concentration on the binding of ANS to protein were compared. The binding between ANS and protein was dependent on pH and ionic strength. It seems that both hydrophobic binding and some electrostatic forces are involved in the binding of ANS to protein. The binding constants for ANS increased with increasing protein concentration. This suggests the possibility of a sharing of one ANS molecule by more than one protein molecule at relatively high protein concentration.

• Food Science of Animal Resources
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• v.26 no.2
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• pp.204-211
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• 2006

This study investigated the effect of salt and glucono-${\delta}$-lactone (GdL) on the cold-set binding of restructured pork washed and pressurized at 200 MPa. Binding strength, PH, water holding capacity (WHC) and color were determined. NaCl improved pH, WHC and binding strength. GdL also increased binding strength while decreased WHC and pH significantly (p<0.05). However, low GdL level combined with NaCl showed high pH and WHC, compared to control. In color, NaCl decreased $L^*$-value with increasing $a^*$-value significantly (p<0.05). In contrast to NaCl, GdL increased $L^*$-value and decreased $a^*$-value. GdL tended to decrease $b^*$-value and significant differences were found when GdL was added above 1%. Pearson's correlation coefficients presented that NaCl had a significant effect on binding strength (0.6632) and lightness (-0.7330) while GdL had a significant correlation with all parameters barring binding strength. The results indicated that under washing and pressure treatments, GdL had a potential effect on cold-set binding with reducing NaCl concentration, especially when low GdL concentration combined with NaCl was added.

• 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.

• Asian-Australasian Journal of Animal Sciences
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• v.19 no.10
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• pp.1484-1489
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• 2006

This study was carried out to investigate the effect of high pressure and the addition of non-meat proteins on the physico-chemical and binding properties of restructured pork. Pressurizations were carried out at up to 200 MPa and non-meat proteins used as a binder were isolated soy protein (ISP), sodium caseinate (SC), whey protein concentrate (WPC) and egg white powder (EWP). The pH values of all treatments were affected by the level of pressure. $L^*$-value of all treatments increased significantly (p<0.05), while both $a^*$-value and $b^*$-value of all treatments showed a significant decrease (p<0.05) with increasing pressure level. Binders could contribute only additive effects on both pH and color of the treatments. It was found that high pressure improved the water binding capacities and binding strength of the treatments. Binders also improved the binding strength of restructured pork. However, SC and WPC had no effect on water binding properties under high pressure. These results indicate that the application of high pressure had more significant effect on restructuring meat than binders.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2006.05a
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• pp.219-223
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• 2006

In the current study, the addition of either NaCl or GdL Increased the binding strength and it considered that the use of GdL with or without low NaCl concentration improved the binding strength of restructured pork meat. Major deterioration of GdL addition is cooked-like discoloration. However, the combination with washing process or addition of carrageenan could improve cold-set binding properties of restructured pork, even if low NaCl or GdL were added.

• Bulletin of the Korean Chemical Society
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• v.17 no.4
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• pp.358-362
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• 1996

The ionic strength dependent binding mode of 9-aminoacridine (9AA), a well-known DNA intercalator, to DNA is studied by flow linear dichroism, circular dichroism, fluorescence techniques and equilibrium dialysis. The DNA-bound 9AA exhibits spectral properties corresponding to the intercalative binding mode disregarding the salt concentrations; the angle between the long-axis transition moment of the 9AA molecule and DNA helix axis is calculated to be about 65°, indicating a significant deviation from the classical intercalation. At low salt concentrations, however, upwards bending curve in Stern-Volmer plot is observed (where 9AA is a fluorophore and DNA a quencher), indicating the coexistence of both static and dynamic quenching mechanisms or the existence of an additional binding site.