• 한국환경과학회지
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• 제6권6호
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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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• 제30권4호
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• pp.341-354
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• 1995

동해의 8개 정점에서 해수 및 추출된 용존 유기물의 형광특성과 아미노산 조성이 연구되었다. C-18 Sep-Pak cartridge에 의해 추출된 시료는 3차원 형광특성 분석에 따 라 생거대물질과 지구거대물질로 구분되었다. 전 조사 정점을 통하여 생거대물질(ex : 280 nm/em : 330 nm)은 표층이 높고 수온약층 아래에서 점차 감소하는 것으로 나타났 으며 이는 표층혼합층의 생물 활동에서 기인된 분해가능한 생거대물질이 수온약층 부 근 및 저층에서 활발한 미생물 분해과정에 의해 감소하는 것으로 사료된다. 한편 이와 는 역상관계를 보이는 지구거대물질 (ex : 330 nm/em : 430 nm)은 표층은 낮고 수온약 층 아래에서 증가하였는데 이는 표층에서 생성된 생거대물질 및 입자유기체가 생물 분 해 후 재축합 과정을 거쳐 난분해성의 지구거대물질로 전환된 것으로 사료된다. HPLC 를 이용하여 해수와 추출된 유존유기물의 아미노산 조성을 분석하였다. 분석결과 Glycine, serine 그리고 alanine등이 우점하였으며, 전체 농도의 50% 이상을 차지하는 것으로 조사되었다. 해수중의 용존 자유아미노산 농도는 표층이 0.7∼1.8um 범위로 저 층 0.2∼0.4um보다 높게 측정되었다. 추출된 유기물중 alanine의 D/L racemice ratio 측정결과 저층보다 표층이 상대적으로 낮은 값을 보였으며 이는 표층의 생거대물질이 연령이 젊고 재순환이 빠르며 생물 분해가능성이 큰 물질임을 시사하고 있다.

• 약학회지
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• 제27권4호
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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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• 제7권1호
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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.

• 약학회지
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• 제32권3호
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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.

• 약학회지
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• 제26권2호
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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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• 제4권2호
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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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• 제6권1호
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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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• 제6권1호
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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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• 제7권2호
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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.