• 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.

• Conservation Science in Museum
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• v.12
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• pp.9-17
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• 2011

This study examined non-destructive UV-Vis spectrophotometry as well as 3-D fluorescence spectrophotometry of textile that made use of red dye such as Sappan wood, madder, Safflower, Gromwell. The authors produced two textile specimen that were dyed by not only two kinds of textile (cotton and silk) but also three kinds of mordanting (no-mordanting, alumen and iron), and they investigated effects of each dye material upon investigation results. At analysis with UV-Vis spectrophotometry of dyed textile specimen, dyeing made by sappan wood, madder and gromwell had significant difference depending upon mardant regardless of kinds of textile, and safflower had no significant difference depending upon textile and mordant. At analysis with 3D-fluorescence spectrophotometry, specimen dyed with sappan wood had difference with mordants, and with madder, there were difference with textiles, and safflower had inherent fluorescence spectrum regardless of textiles and mordants, while gromwell had no fluorescence spectrum.

• Archives of Pharmacal Research
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• v.7 no.1
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• pp.11-15
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• 1984

Binding of sic cephalosporins (cefotaxime, cefuroxime, cafazoline, cephalothin, cephaloridine, cephacetrile) to human serum albumin was studied. Fluorescence probe technique and difference spectrophotometry were employed to evaluate the nature and degree of association of cephalosporin-albumin complex. 1-anilinonaphthalene-8-surfonate was used as the fluorescence probe, and 2-(4'-hydroxybenzeneazo)benzoic acid as the UV spectrophotometric probe. Competitive bindings between cephalosporins and probe were observed. For the binding of cephalosporins to human serum albumin, three binding sites were identified by fluorescence probe technique but four binding constants of cephalosporins to human serum albumin measured by fluorescence probe technique are higher than those meausred by UV spectrophotometry.

• Textile Coloration and Finishing
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• v.17 no.6 s.85
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• pp.27-35
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• 2005

Conventional pad- dry-cure(thermo-fixation) process usually produces functional performance on both sides of a fabric. UV curing technique was applied to impart water- and oil-repellent finish effective only on the face of a PET knitted fabric. The preferential one-side coating, by virtue of the limited penetration of UV light, was achieved by W curing after padding of a fluorocarbon agent without special coating or printing equipments. The difference in the functional property of face and back sides was examined by measuring water and oil repellency at each side of the treated fabric. The influence of pre/post-irradiation dose and agent concentration on the performance of the finished fabrics were investigated. While increase in both resin concentration and post-irradiation did not have significant effect on the finish, UV pre-irradiation of PET fabrics caused remarkable influence presumably due to appropriate surface modification of PET fabrics required for facile wetting of the resin. The dimensional stability and color change of the UV cured fabrics measured by FAST and reflectance spectrophotometry showed significantly decreased color difference and increased percent extension compared with the samples pre-irradiated without agent application.

• YAKHAK HOEJI
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• v.35 no.1
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• pp.1-6
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• 1991

Fast Hartley transform(FHT) was used for the identification of derivative UV spectra of pharmaceuticals, with the advantages of relatively shorter computing time of FHT and more precise results. The arccosine value of dot product of two vectors of normalized FHT coefficients calculated from two compared derivative spectra was a reasonable parameter for the spectral identification. Using this parameter, the similar patterns of derivative spectra of 13 penicillins can be differenciated from each other. The concentration difference and the minor contamination did not interfere the results of identification procedures. All these procedures of identification were accomplished successfully by the computer program, [SPECMAN PLUS] version 1.30, which was developed for this article.

• YAKHAK HOEJI
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• v.32 no.3
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• pp.182-186
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• 1988

Binding of four cephalosporins(cefaclor, cefpiramide, ceftazidime, ceforanide) to bovine serum albumin was studied. Difference spectrophotometry was employed to evaluate the nature and the degree of association of cephalosporin-albumin complex. 2-(4'-hydroxybenzen azo) benzoic acid was used as the uv spectrophotometric probe for measuring the binding of cephalosporins to bovine serum albumin. Competitive bindings between cephalosporins and probe were observed. For the binding of cephalosporins to bovine serum albumin, three binding sites were identified. The binding constants of cefaclor, ceforanide, ceftazidime and cefpiramide were $12.57\;{\times}\;10^{-2}M^{-1}$, $6.49\;{\times}\;10^{-2}M^{-1}$, $4.70\;{\times}\;10^{-2}M^{-1}$ and $6.20\;{\times}\;10^{-2}M^{-1}$ respectively.

• Archives of Pharmacal Research
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• v.6 no.1
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• pp.55-62
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• 1983

Binding of six cephalosporins (cefotaxime, cefuroxime, cefazoline, cephalothin, cephaloridine, cephacetrile) to bovine serum albumin was studied. Fluorescence probe technique and difference spectrophotometry were employed to evaluate the nature and degree of association of cephalosporin albumin complex. 1-Anilinonaphthalene-8-sulfonate (ANS) was used as the fluorescence probe. 2-(4'-hydroxybenzeneazo) benzoic acid(HBAB) was employed as the UV spectrophotometric probe. Compentitive bindings between cephalosporins and probes were observed. The number of binding sites of bovine serum albumin for each cephalcsporin is 2. Among six cephaloporins, cefotaxime has the highest binding constant followed by cafazoline, cefuroxime, cephalothin, cephaloridine and cephacetrile.

• Journal of Pharmaceutical Investigation
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• v.17 no.1
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• pp.1-14
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• 1987

To increase the bioavailability of norfloxacin, inclusion complex of antimicrobial agent norfloxacin with ${\beta}-Cyclodextrin$ was prepared and studied by the solubility method, spectrophotometric methods(UV, IR, $^1H-NMR$), differential thermal analysis, powder X-ray diffractometry, the physical properties, the antimicrobial activity, DNA binding and in situ recirculation technique. The conclusions are summerized as following; 1) The inclusion complexation was identified by means of solubility, spectrophotometry(UV, IR, NMR), DTA and X-ray diffraction. 2) The molar ratio of $norfloxacin-{\beta}-cyclodextrin$ complex was 1 : 1. 3) The stability constant of $norfloxacin-{\beta}-cyclodextrin$ complex was $21.5\;M^{-1}$, and both true and apparent partition coefficients of the inclusion complex were larger than those of norfloxacin. 4) The time required to dissolve 60% $(T_{60}%)$ of the inclusion complex was 120 min. in distilled water and in the artificial intestinal juice, while norfloxacin did not reach to 60% dissolution within 120 min. 5) The antimicrobial activity of the inclusion complex against Pseudomonas aeruginosa, Klebsiella pneumoniae and Staphylococcus aureus showed no significant difference compared to that of norfloxacin alone. 6) Studies on binding properties between the inclusion complex and norfloxacin alone to DNA according to equilibrium dialysis showed no significant differency. 7) In situ absorption rates (Ka) of inclusion complex and norfloxacin alone were 0.229 and $0.102hr^{-1}$, respectively.

• Conservation Science in Museum
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• v.11
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• pp.61-72
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• 2010

This is the analysis of material dyed with Korean yellow dyes such as tumeric, amur cork tree, goldthread, gardenia, and the flowers of sophora japonica using nondestructive ultraviolet-visible and fluorescence spectrophotometry. In order to find out whether type of fabric or mordant influences analysis results, test fabrics were made using two types of fabric(silk and cotton) and dyed using three different mordants(no mordant, alum, iron). After analysis with UV-Vis reflectance spectrum on the dyed fabric, when the fabric was dyed with tumeric, amur cork tree and goldthread, the results were similar with no mordant and alum mordant, whereas there was a difference with an iron mordant. Also when the fabric was dyed using gardenia, different fabrics brought different results but there was no difference in results with mordants. On the other hand, when the fabric was dyed using the flowers of sophora japonica, there was no difference with fabrics but with mordants. After analysis with 3D-fluorescence spectrum, fabrics dyed with tumeric, amur cork tree and goldthread showed their own fluorescent spectrum with no regard to fabric and mordant; but with gardenia, there were differences with different fabrics whereas with the flowers of sophora japonica, there were differences with mordants.

• 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.