• Bulletin of the Korean Chemical Society
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• v.23 no.1
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• pp.29-34
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• 2002

The microphase adsorption - spectral correction (MPASC) technique was described and applied to study the interaction of fluorescein isothiocyanate (FITC) with cetyl trimethylammonium bromide (CTAB). The synergism mechanism of micelle was analyzed and discussed. The aggregation of FITC on CTAB obeys the Langmuir monolayer adsorption. Results showed that the monomer and micellar aggregate is $FITC-CTAB_3$ and $(FITC-CTAB_3)_{29}$, respectively at pH 9.62. The adsorption constant of the CTAB-FITC aggregate was determined to be $2.10{\times}10^5$. Interestingly, it was observed for the addition of an anionic surfactant to desorb FITC from its CTAB aggregate and this has been applied to the quantitative determination of trace amounts of anionic detergent (AD) in sewage.

• Journal of Photoscience
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• v.10 no.3
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• pp.237-240
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• 2003

The tetradecameric peptide (K47-K60) near the NH$_2$-terminal region of epithelial-cell adhesion molecule (Ep-CAM) was chosen as antigenic site and a polyclonal antibody was generated, which could recognize Ep-CAM from the mouse colon tissue or the colon cancer cell, CT-26, in Western blot analysis. Then, the fluorescein isothiocyanate (FITC), a fluorescence dye, was conjugated with the affinity purified Ep-CAM antibody using thiocyanate and the amino groups of FITC and antibody, respectively. The molar ratio of FITC to antibody was estimated approximately 1.86 to 1.00 by measuring the optical densities at 492 nm and 280 nm. Ep-CAM antibody-FITC conjugate was then used for immunohistochemistry of the CT-26 cells. Judging from the shapes formed by fluorescence, the Ep-CAM antibody could delivered FITC to the surface of cells in which Ep-CAM was expressed. This result implies that Ep-CAM antibody could be also used for the tissue-specific delivery of the photosensitizer to the target protein via antigen-antibody interaction.

• Bulletin of the Korean Chemical Society
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• v.34 no.2
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• pp.539-544
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• 2013

$Ag@SiO_2@SiO_2$(FITC) nanocomposites were prepared by the simple polyol process and St$\ddot{o}$ber method. Fluorescence enhancement of fluorescein moiety (fluorescein isothiocyanate, FITC) was investigated in the presence of silver nanoparticles in $Ag@SiO_2@SiO_2$(FITC) system with varying thickness (X nm) of first silica shell. Maximum enhancement factor of 4.3 fold was achieved in $Ag@SiO_2@SiO_2$(FITC) structure with the first silica shell thickness of 8 nm and the average separation distance of 11 nm between the surface of silver nanoparticle and fluorescein moiety. The enhancement is believed to be originated from increased excitation rate of fluorescein moiety due to concentrated local electromagnetic field which was improved by interaction of light with silver nanoparticles.

• Food Science and Biotechnology
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• v.17 no.6
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• pp.1365-1367
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• 2008

The antibacterial activity of chitosan against Escherichia coli was investigated in the presence of NaCl, sucrose, and ethanol to assess the potential use of chitosan as a biopreservative in food products containing these components. The inhibitory activity of chitosan decreased slightly upon the addition of NaCl and sucrose, respectively to culture broth containing 100 ppm of chitosan (Mw 3,000), while the addition of ethanol enhanced the inhibitory activity of chitosan on growing cells. The addition of these components to non-growing cells prior to chitosan treatment demonstrated that NaCl protected the cells from the inhibitory activity of chitosan, while sucrose had no effect. Ethanol addition to non-growing cells increased cell death by chitosan treatment. Finally, binding of fluorescein isothiocyanate (FITC)-labeled chitosan to E. coli was measured in the presence of the food components. The FITC-labeled chitosan binding to cells decreased upon NaCl addition, was not affected by sucrose, and increased following treatment with ethanol.

• Korean Journal of Plant Tissue Culture
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• v.21 no.6
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• pp.363-367
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• 1994

In an effort to investigate the role of calmodulin (CaM) as a modulating molecule in the signal transduction system in plant cells, we established methods for introduction of purified CaM into cultured soybean cells. CaM was purified from bovine testis, and was labelled with fluorescein isothiocyanate (FITC). Suspension -cultured cells were healed with saponin (0.1 mg/mL) to permeabilize the plasma membrane and coincubated with FITC-CaM complex. Saponin pretreatment was found to increase the fluorescence in the suspension cultured cells, indicating that the FITC-CaM complex could be incorporated into the cytoplasm. Optimal conditions for introducing FITC-CaM complex into protoplasts by electroporation were established with various electric pulses. With increasing field strength, the fluorescence in the protoplase was increased, while the viability of the protoplase decreased. FITC-CaM complex was successfully introduced into the protoplasts by electroporation and the amount of FITC-CaM complex in the protoplase was estimated.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.14 no.8
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• pp.4106-4110
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• 2013

Apolipophorin-III (apoLp-III) was isolated and purified from the last larval hemolymph of Galleria mellonella by the KBr gradient ultracentrifugation and gel chromatography (Sephadex G-100). In this paper, we examined that apoLp-III is taken up into the last larval fat bodies in Galleria mellonella. The last larval fat body tissues were incubated at room temperature for 30 min with fluorescein isothiocyanate (FITC)-labeled apoLp-III (FITC-apoLp-III). Fluorescein microscopy and sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) revealed that the last larval fat body tissues internalize FITC-apoLp-III. The results show that the apoLp-III is taken up by the last larval fat body.

• Polymer(Korea)
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• v.28 no.3
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• pp.232-238
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• 2004

MPEG-PCL diblock copolymers consisting of methoxy poly(ethylene glycol) (MPEG) and $\varepsilon$-caprolactone (CL) as drug carriers were synthesized by ring-opening polymerization MPEG-PCL diblock copolymers were characterized by X-ray diffraction and differential scanning calorimetry. After freeze milling of block copolymers and albumin bovine-fluorescein isothiocyanate (FITC-BSA) as model protein, the wafers loaded FITC-BSA were fabricated by direct compression method. The release profiles of FITC-BSA were examined using pH 7.4 PBS for 14 days at 37$^{\circ}C$. The release amount was determined by fluorescence intensity by using the fluorescence spectrophotometer. The morphological change of wafers was observed by digital camera and scanning electron microscope. The release rate and initial burst of BSA increased with increasing PEG molecular weights and decreasing PCL molecular weights in the segments of MPEG -PCL diblock copolymers.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.17 no.10
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• pp.199-203
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• 2016

Apolipophorin-III (apoLp-III) was isolated and purified from the last larval hemolymph of Galleria mellonella by KBr gradient ultracentrifugation and gel chromatography (Sephadex G-100). After KBr gradient ultracentrifugation, the lipophorin-free fractions were used as the samples for gel chromatography. The purity of the finally purified apoLp-III was confirmed by SDS-PAGE after gel chromatography. In this study, we found that apoLp-III is taken up into the adult testes in Galleria mellonella. The testes were dissected from day-1 or -2 adults in cold Ringer's solution and used for tissue culture. The protein moiety of apoLp-III was labeled with FITC dissolved in dimethyl sulfoxide (DMSO) at room temperature under conditions of continuous stirring for 1 h. The FITC-labeled apoLp-III was purified with a Sephadex G-25 PD-10 column. The tissues of the adult testes were incubated at room temperature for 30 min with fluorescein isothiocyanate (FITC)-labeled apoLp-III. Fluorescein microscopy and sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) revealed that the adult testis tissues internalize the FITC-labeled apoLp-III. The results showed that apoLp-III is taken up by the adult testes.

• Development and Reproduction
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• v.11 no.1
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• pp.21-29
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• 2007

Previously, we found progesterone receptor membrane component 2 (pgrmc2) was highly expressed in germinal vesicle (GV) stage oocytes. The present study was conducted to characterize the expression of pgrmc2, as well as pgrmc1, in the mouse gonads and embryos according to their developmental stages. We found that these membrane components were expressed in ovaries, testes, and embryos at various developmental stages in addition to oocytes. Progesterone-3-O-carboxymethyl oxime-BSA-fluorescein isothiocyanate (P4-BSA-FITC) was applied to visualize the presence of the progesterone receptor on mouse oocyte membrane, and we confirmed that immobilized progesterone is localized at surface of the oocyte. This is, at our knowledge, the first report regarding the expression of membrane component of progesterone receptor in the mouse oocytes, embryos, and gonads. The function and signal transduction pathway of progesterone receptor membrane components in oocytes requires further studies.

• Polymer(Korea)
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• v.34 no.1
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• pp.79-83
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• 2010

Alginate beads were prepared using poly(N-isopropylacrylamide-co-dimethylamino ethyl methacrylate)(P(NIPAM-co-DMAEMA)). First, P(NIPAM-co-DMAEMA) was immobilized on the surface of alginate beads by taking advantage of electrostatic interaction between alginate and P(NIPAM-co-DMAEMA). Second, P(NIPAM-co-DMAEMA) was contained in the matrix of alginate beads. P(NIPAM-co-DMAEMA) were prepared by a free radical polymerization at $74^{\circ}C$ for 12 h. The weight ratio of NIPAM to DMAEMA monomer was 95/5. The copolymer was identified by $^1H$-NMR. Releases from the alginate beads were observed at 30, 37, and $45^{\circ}C$ using blue dextran or FITC-dextran(fluorescein isothiocyanate-dextran) as a model drug. The effect of temperature on the degree of release from the beads was insignificant. FITC-dextran was released more than blue dextran possibly due to its smaller molecular weight.