• Macromolecular Research
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• v.12 no.3
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• pp.282-289
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• 2004

We have extensively characterized the fluorescence behavior of unsaturated polyester (UP) resin in the absence and presence of a 1,3-bis-(l-pyrenyl)propane (BPP) fluorescent probe at various dynamic and isothermal cure histories by means of a steady-state fluorescence technique using a front-face illumination equipment. In addition, we explored the effect of the fluorescence intensity on the relaxation of the fluorescent probe in the UP resin by resting the dynamically and isothermally cured resin at ambient temperature and pressure for 24 h. The monomer fluorescence intensity, which has two characteristic peaks at 376 and 396nm, changed noticeably depending on the cure temperature and time and provided important information with respect to the molecular and photophysical responses upon curing. The result of the fluorescence study indicates that the increased local viscosity and restricted molecular mobility of the UP resin surrounding the BPP probe after curing are both responsible for the enhancement of the monomer fluorescence intensity. Our results also demonstrate that once the BPP probe has enough time to rearrange and become isolated prior to fluorescence, a sufficient amount of fluorescence is emitted. Therefore, we note that the fluorescence behavior of this UP resin system is influenced strongly by the relaxation process of the fluorescent probe in the resin as well as process used to cure the resin.

• 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.

• Archives of Pharmacal Research
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• v.8 no.4
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• pp.205-211
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• 1985

The distribution of local anesthetics between the hydrocarbone interior and surface area of the lipid bilayer of liposomal membrane was calculated employeg fluorescence probe technique. The quenching of fluorescence probe technique. The quenching of fluorescence probe technique. The quenching of fluorescence of 12-(9-anthroyl) stearic acid and N-octadecyl naphthyl-2-amini-6-sulfonic acid by the local anesthetics in liposomal system was used to calculate the distribution. The Stern-Volmer equation was modified and employed for this calculation. The results showed that procaine hydrocloride and benzocaine were mainly distributed on the surface area of the lipid bilayer of the liposoal membrane, while tetracaine hydrochloride penetrated effectively into the hydrocarbon interior and showed even distribution in the lipid bilayer.

• Proceedings of the Optical Society of Korea Conference
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• 2007.07a
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• pp.35-36
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• 2007

We report a probe using a single double clad fiber (DCF) for fluorescence spectroscopy. Bidirectional separate transmission for excitation and fluorescence light in a single fiber was implemented. A DCF coupler made by side-polished method could extract none but the collected fluorescence signals propagating in inner cladding mode, thereby diminishing the interference of silica background generated by the excitation in core mode. The experimental results show that the fluorescence spectra of biological tissues obtained using the DCF probes have much less silica background than using a standard multiple-mode fiber.

• 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.

• Journal of the Korean Society for Precision Engineering
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• v.25 no.5
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• pp.140-147
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• 2008

In this study, a carbon nanotube probe (CNT probe) is proposed as a mechanical force transducer for the measurement of pico-Newton (pN) order force in biological applications. In order to measure nantube's displacement in the air or liquid environment, the fabrication of a CNT probe with tip-specific loading of fluorescent dyes is performed using tip- specific functionalization of the nanotube and chemical bonding between dyes and nanotube. Also, we experimentally investigated the mechanical properties of the CNT probe using electrostatic actuation and fluorescence microscope measurement. Using fluorescence measurement of the tip deflection according to the applied voltage, we optimized the bending stiffness of the CNT probe, therefore determined the spring constant of the CNT probe. The results show that the spring constant of CNT probes is as small as 1 pN/nm and CNT probes can be used to measure pN order force.

• Proceedings of the KSAR Conference
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• 2003.06a
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• pp.24-24
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• 2003

Fluorescence in situ Hybridization(FISH)는 특정 염기서열을 이용하여 염색체나 염색체상의 DNA위치를 확인하는 기술로서, 면역세포화학 기술과 결합되어져 현미경으로 이들의 유전적 활성도를 직접 확인할 수 있는 방법으로 지금까지의 radioisotopes 대신 non-radioactive labeling 방법으로서 fluorescence을 이용한 분자세포유전학적 검정 방법이다. 따라서 특정 염색체의 FISH probe의 개발은 FISH 기법을 이용하여 조직 또는 세포내 특정 염색체나 DNA의 존재나 이상 유무를 신속하고 정확하게 파악할 수 있다. 본 연구는 소와 사람을 대상으로 Y-염색체 특이 DNA probe를 개발하고 이를 이용하여 FISH를 시행함으로서 본 probe의 신뢰성을 확인하고 임상적 적용 가능성을 제시 하고자 하였다.

• 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 the Korean Society of Food Science and Nutrition
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• v.24 no.3
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• pp.446-453
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• 1995

The improtant components of extracellular matrix(ECM) are collagen and chondroitin sulfate. The hydrophobic surface of collagen is one of the determining factors of diameter of collagen fiber and also is closely related to the aging phenomena. The controlling mechanism of the diameter of collagen fiber influenced by the interaction with chondroitin sulfate was evaluated using bis-ANS as a hydrophobic probe. Hydrophobic surface area of collagen molecule shielded by chondroitin sulfate was evaluated. Relative fluorescence intensity of collagen in thepresence of chondroitin sulfate was measured using bis-ANS as a hydrophobic probe. The fluorescence intensity decreased with the increase in chondroitin sulfate up to 3.8 chondroitin sulfate/collagen(mole/mole). Further increase in the ratio of chondroitin sulfate to collagen did not change the fluorescence intensity. Similar changes in the relative fluorescence intensity were observed for both rat tail and lathyrific rat skin collagen. The fluorescence intensity indicated by the binding between bis-ANS and hydrophobic sites of collagen was pH dependent, and the shielding effect of collagen-chondroitin sulfate interaction could not be detected at pH above 6.0. This is probably due to the charge repulsions caused by negative charged collagen molecules at higher pH.

• Proceedings of the Korean Society of Precision Engineering Conference
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• 2008.06a
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• pp.97-98
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• 2008