• Journal of Environmental Science International
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• v.6 no.6
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• pp.595-604
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• 1997

To investigate characteristics of biogeochemical environment of the Korea Deep Ocean Study(KODOSI area in the northeast Pacific Ocean, we preferentially measured Inorganic nutrients and fluorescent organic matters. Typically. the permanent thermocline was well developed at the depth of 200~1000m In the study area. Nitrate. phosphate and silicate were low In the surface mixed layer and Increased with depth. N/P and N/Si showed 15 and 0.2 respectively In the deeper layer. Two fluorophores, biomacromolecule(protein-like) and geomacromolecule (humid-like) , were observed by three dimensional fluorescence excltatlon/ emission spectra matrix. Biomacromolecule(maximum fluorescence at $Ex_{280m}/Em_{330nm}$) ranged from 41.9 to 147.0 TU with its maximum In the surface mixed layer and minimum in deeper water, This is a same trend that has been reported for DOC in the equatorial Pacific. This suggests that biomacromolecule might be labile and converted to refractory humic substance after bacterial degradation In the deeper layer. On the contrary, geomacromolecule(maximum fluorescence at $Ex_{330m}/Em_{430m}$), ranged from 7.6 to 46.5 QSU, showed minimum in the surface nixed layer(euphotic zone) Implying photodegradation and then increased with depth at all stations. In the characteristics of vertical profiles, the relationship between biomacromolecule and geomacromolecule showed negative correlation. Such trend can be attributed to biochemical regeneration or formation of fluorescent materials accompanying oxidation and rennnerallzation of settling organic matter.

• 한국해양학회지
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• v.30 no.4
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• pp.341-354
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• 1995

Fluorescence characteristic and amino acids composition of organic matter were determined from extracted seawater samples at eight stations in the East Sea of Korea. Organic compounds have been extracted onto C-18 Sep-Pak cartridges. Three dimensional excitation/emission fluorescence contouring of extracts showed two markedly distinct characterized fluoroscopies representing protein-like biomacromolecule and humic-like geomacromolecule. Protein-like biomacromolecule showing fluorescence maxima at 280 nm/330 nm (excitation/emission) were abundant in the surface mixed layer and then apparently decreased below the thermocline at most stations. It suggests that source of biomacromolecule is comely related with vigorous biological synthetic activity in the surface layer and bacteria decompose its biologically labile components near the thermocline and in the deeper layer. On the other hand, humiliate geomacromolecule showing fluorescence maxima at 330 nm/430 nm (excitation/emission) were low in the surface mixed layer implying photochemical oxidation and then increased below the thermocline at most stations. It suggests that geomacromolecule might be transformed by condensation of bio-refractoryorganic fraction after decomposition of biomacromolecule and particulate organic carbon derived from the surface mixed layer. HPLC measurements of amino acids showed similar composition between seawater and extracted organic macromolecule after hydrolysis. Glycine, serine and alanine were predominant, accounting for more than 50% of total amino acids. Dissolved free amino acids of seawater were more abundant in the surface layer(0.7∼1.8 uM) than the deeper layer (0.2∼0.4 uM). D/L racemic ratio of alanine of extracted organic matter showed lower value in the surface layer than the deeper layer. It suggests that biomacromolecule predominant in the surface layer is relatively young, rapidly recycling and biologically labile.

• YAKHAK HOEJI
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• v.27 no.4
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• pp.257-261
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• 1983

Binding of nalidixic acid which is used primarily in the treatment of urinary infection and probenecid which is used as a uricosuric agent to bovine serum albumin were studied using difference spectrophotomeric method. 2-(4'-Hydroxybenzeneazo) bcnzoic acid as a spectrophotometric probe was used for measuring the binding of nalidixic acid and probenecid to bovine serum albumin. The association constants of nalidixic acid and probenecid were $1.58{\times}10^{4}M^{-1}$ and $1.70{\times}10^{4}M^{-1}$, respectively.

• 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.

• 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.

• 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.

• 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.

• 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.

• Archives of Pharmacal Research
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• v.6 no.1
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• pp.63-68
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• 1983

The binding properties of three ginsenosides, Rb$_{1}$, Rc and Re, to bovine and human serum albumins have been examined by fluorescence probe technique. 1-anilinonphathalene-8-sulfonate (ANS) was used as the fluorescence probe. Protopanaxatriol glycoside, Re, did not quench the fluorscence of ANS to the bovine serum albumin. Competitive bindings between protopanaxadiol glycosides, Rb$_{1}$ and Rc are both 3.3 . The binding constants for Rb$_{1}$ and Rc with bovine serum albumin were 1.91 * 10$_{4}$M$_{-1}$ AND 1.04 * 10$^{[-994]}$ M$^{-1}$ , respectively. The ginsenosides, Rb$_{1}$, Rc and Re did not quench the fluorescence of ANS bound to human serum albumin.

• 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.