• Title/Summary/Keyword: Chloramine

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Radioiodine Labeling of Insulin Using Dimethylsulfoxide as a Labelling-Aid

  • Kim, Jaerok;Kim, Young-Hee
    • Nuclear Engineering and Technology
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    • v.9 no.4
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    • pp.203-210
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    • 1977
  • Using dimethylsulfoxide (DMSO) as a labelling aid, insulin--$^{126}$ I of radioimmunoassay use has been effectively prepared. A small amount of DMSO was added to usual labelling mixture ana the reaction time was controled. The labelled insulin obtained in such a way showed improved bindabilities to the antibody and thus expressed larger dose-gradients in the plots of standard dose-response curves even though the labelling rate was decreased to some extent. However, by extending the reaction time to about 1 min, average labelling yield of 30% could be obtained. The average increase of bindability (B/F) in definite antiserum dilution was 2.5 comparing with 1.5 obtained in the absence of DMSO. Thus, the net bindability increase was 70% of those obtained in tile absence of DMSO. By means of a NMR spectrometry, it has been confirmed that the DMSO in the labelling mixtutre is converted to dimethylsulfone by chloramine-T. The results, generally agreed with the Stags's postulation, were discussed in view of a competitive oxidation of DMSO with disulfide linkages of the insulin molecule by the chloramine-T.

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Management of Swimming Pool (수영장 관리)

  • Kim Kyong-Ho
    • Journal of environmental and Sanitary engineering
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    • v.4 no.1 s.6
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    • pp.37-42
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    • 1989
  • Management of Swimming pool is focused on Swimming pool samitation in relation with chlorination of swimming water and potable water, disposal of waste and excrement within the boundry of swimming pool that may be summerised as follows: 1. Chlorination of Swimming Water Residual chlorine must be kept within the range of $0.4\~0.6 mg/l$ and in case of chloramine should be $0.7\~1.0mg/l$ while swimming pool is in operation 2. Chlorination of potable Water Residual chlorine must be kept within the rangs of $0.2\~04 mg/l$ at all time 3. Disposal of litters must be kept in the water tight waste bin with fitted lid, and waste should not be overflow -out of the bin. When waste in landfilled, the sufficient amount of cover material should be used daily. 4. Disposal of excrement Toilet must be water-flush type. However, The establishment of pit latrine is unavoidable the excrement must be covered with lime or dirt so that excrement should not be exposed to air.

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Studies on Setting up of Radioimmunoassay System of Thyroid Stimulating Hormone (갑상선자극(甲狀腺刺戟)호르몬의 방사면역측정법(放射免疫測定法) 확립(確立)에 관한 연구(硏究))

  • Kim, Jae-Rok;Park, Kyung-Bae;Awh, Ok-Doo
    • The Korean Journal of Nuclear Medicine
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    • v.20 no.1
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    • pp.75-83
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    • 1986
  • Various TSH RIA kit components were prepared. Conditions for $^{125}I$ labelling of h-TSH were optimized by diminishing the amount of chloramine-T, ertending reaction time and lowering reaction temperature. Yield, specific activity, and immunological activity could be maintained moderately under such mild reaction conditions. The mixture of polyethyleneglycol(PEG) and second antibody worked effectively as a B/F separation agent. Even though the mixture was made with more diluted PEG and second antibody than those of using the sole component separately, the tine required for the B/F separation was shorter in case of using the mixture. The sequential saturation technique was efficient than those of applying ordinary equilibrium saturation technique in assay sensitivity and assay precision points of view.

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Studies on the Radioimmunoassay of Human Growth Hormone - 1. Evaluation of the method of determination (사람성장(成長)홀몬의 방사면역측정(放射免疫測定)에 관한 연구 - 제I편 사람성장(成長)홀몬의 측정법에 관한 검토)

  • Lee, Young-Woo;Lee, Hong-Kyu;Koh, Chang-Soon;Lee, Mun-Ho
    • The Korean Journal of Nuclear Medicine
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    • v.6 no.1
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    • pp.17-24
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    • 1972
  • Utilizing the commercial radioimmunoassay kit, the author assayed HGH and evaluated the problems of the method. The method had the sensitivity of 0.5 mug/ml degree and could determine the plasma HGH concentration directly without the help of plasma extraction. Also it was specific for the HGH, when tested by a dilution method using test utilizing the plasma of the acromegalic patient. The author also obtained the $^{125}I$ labelled HGH of specific activity of $156.3{\mu}Ci/{\mu}g$, performing the chloramine-T method.

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Establishment of I-131, Tc-99m Labeling Methods to In-house Anti-CEA Antibodies and Evaluation of the Immunological Characteristics (국산 항 CEA 항체의 I-131, Tc-99m 표지법 확립 및 면역학적 특성 분석)

  • Chung, June-Key;Lee, Dong-Soo;Lee, Myung-Chul;Chung, Hong-Keun;Koh, Chang-Soon;Hong, Mee-Kyoung;Choi, Seok-Rye;Seo, Il-Taek;Chung, Jun-Ho
    • The Korean Journal of Nuclear Medicine
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    • v.26 no.2
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    • pp.346-354
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    • 1992
  • Cancer cells have several tumor-associated antigens on the cell surfaces, and antibodies against these antigens have been developed by many investigators. Radiolabeled antibodies have been used as new methods to diagnose and treat malignant tumors. Especially anti-carcinoembryonic antigen (CEA) is the most popular antibody for these purposes. In this investigation, we tried to label $^{131}I$ and $^{99m}Tc $ to anti-CEA monoclonal antibodies which were developed in the Seoul National University College of Medicine. We found CEA-79 and CEA-92 antibodies had the better immunological characteristics among 8 anti-CEA monoclonal antibodies. And radioiodination of CEA-79 could be performed by chloramine-T method, while radioiodination of CEA-92 by iodogen method. To label these antibodies with $^{99m}Tc $, we used pretargeting transchelation as direct labeling method. At first, $^{99m}Tc $ was bound to glucaric acid, and monoclonal antibody was reduced by $\beta-mercaptoethanol$. When these were incubated together. $^{99m}Tc $ bound to glucarate was switched to monoclonal antibody because of higher affinity. We established conditions of several steps in this method. Anti-CEA monoclonal antibodies labeled with $^{131}I$ and $^{99m}Tc $ are expected to be used valuably in the detection and treatment of malignant tumors.

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A study on the Active Site of Cytidine Deaminase from Bacillus subtilis ED 213 by Chemical Modification (화학적수식에 의한 Bacillus subtilis ED 213 Cytidine Deaminase의 활성부위에 관한 연구)

  • Park, Jung-Moon;Park, Sang-Won;Suh, Tae-Soo;Kim, Jung;Yu, Tae-Shick
    • Korean Journal of Microbiology
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    • v.35 no.2
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    • pp.133-138
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    • 1999
  • Essential amino acids involving in the active site ofthe cytidn~e deruninase from Bncillus subtilis ED 213 were determined by chemical modification studies. Tllc purified cytidine deruninase tiom Booillus subtilis ED 213 required the reduced form of Fe(lI)ion. since the enzyme was inhibited 43% by 1 mnM o-phenanthroline. Whereas the enzyme activity was activated up to 28% by 1 1 ethylenediaminetetraacetic acid. The cytidine deaninase activily was completely inhibited by 1 mM N-bromosuccinimide, chloramine-T, and p-chloromercuribenzoic acid (p-CMB), respectively. The enzyme activity was inhibited 36% by 1 mM pyridoxal-S-phosphale, and 31% by 1 mM l-ethy~-3-(3-dirneIhj~laminoprop}~~)c~bodiiamide and glycine inethyl ester. The enzyme activity was strongly inhibited 68% by 1 \mu$M \rho$-CMB and this inhibition of the enzyme activity with 1 \mu$M \rho$-CMB was completely reactivated by 5 mM cysleine as a reducing agent. We speculaled that tyrosine, methionine, cysteuie and/or serine residues are located ui or near ihe active site of the cytidine deruniuase from Bncilus subrilis ED 213 and indirectly related to lysine and/or glycine.

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Radiosynthesis of 125I-labeled 2-cyanobenzothiazole: A new prosthetic group for efficient radioiodination reaction

  • Mushtaq, Sajid;Choi, Dae Seong;Jeon, Jongho
    • Journal of Radiopharmaceuticals and Molecular Probes
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    • v.3 no.1
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    • pp.44-51
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    • 2017
  • Herein we report an efficient radiolabeling method based on a rapid condensation reaction between N-terminal cysteine and 2-cyanobenzothiazole (CBT). Radioiodination of 2-cyano-6-hydroxybenzothiazole 2 was carried out using chloramine-T to give $^{125}I$-labeled CBT ([$^{125}I$]1) with a high radiochemical yield ($90{\pm}6%$ isolated yield, n=3) and radiochemical purity (>99%). To evaluate the radiolabeling efficiency of $^{125}I$-labeled CBT, model compounds, L-cysteine and N-terminal cysteine conjugated cRGD peptide were reacted with [$^{125}I$]1 under mild conditions. The radiolabeling reactions rapidly provided the $^{125}I$-labeled products [$^{125}I$]5 and [$^{125}I$]6 with excellent radiochemical yields and radiochemical purity. Therefore, we demonstrate that [$^{125}I$]1 will be a useful prosthetic group for radioactive iodine labeling of N-terminal cysteine bearing biomolecules.

Synthesis of 125I-labeled tetrazine for efficient radiolabeling of human serum albumin

  • Shim, Ha Eun;Jeon, Jongho
    • Journal of Radiopharmaceuticals and Molecular Probes
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    • v.3 no.2
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    • pp.98-102
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    • 2017
  • We demonstrate a detail protocol for the radiosynthesis of a $^{125}I-labeled$ tetrazine prosthetic group and its application to the efficient radiolabeling of trans-cyclooctene-group conjugated human serum albumin (3) using inverse-electron-demand Diels-Alder reaction. Radioiodination of the stannylated precursor (2) was carried out by using [$^{125}I$]NaI and chloramine T as an oxidant at room temperature for 15 min. After HPLC purification of the crude product, the purified $^{125}I-labeled$ azide ([$^{125}I$]1) was obtained with high radiochemical yield ($65{\pm}8%$, n = 5) and excellent radiochemical purity (>99%). Inverse-electron-demand Diels-Alder reaction between ([$^{125}I$]1) and 3 gave the $^{125}I-labeled$ human serum albumin ([$^{125}I$]4) with more than 99% of radiochemical yield as determined by radio-thin-layer chromatography (radio-TLC). These results clearly indicate that the present radiolabeling method will be useful for the efficient and convenient radiolabeling of trans-cyclooctene-group containing biomolecules.

Chemical Modification of Intracellular Cytosine Deaminase from Chromobacterium violaceum YK 391

  • Kim, Jung;Kim, Tae-Hyun;Yu, Tae-Shick
    • Biotechnology and Bioprocess Engineering:BBE
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    • v.10 no.3
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    • pp.180-185
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    • 2005
  • Cytosine deaminase (cytosine aminohydrolase, EC 3.5.4.1) stoichiometrically catalyzes the hydrolytic deamination of cytosine and 5-fluorocytosine to uracil and 5-fluorouracil, respectively. Amino acid residues located in or near the active sites of the intracellular cytosine deaminase from chromobacterium violaceum YK 391 were identified by chemical modification studies. The enzymic activity was completely inhibited by chemical modifiers, such as 1mM NBS, chloramine-T, $\rho-CMB,\;\rho-HMB$ and iodine, and was strongly inhibited by 1mM PMSF and pyridoxal 5'-phosphate. This chemical deactivation of the enzymic activity was reversed by a high concentration of cytosine. Furthermore, the deactivation of the enzymic activity by $\rho-CMB$ was also reversed by 1mM cysteine-HCI, DTT and 2-mercaptoethanol. These results suggested that cysteine, tryptophan and methionine residues might be located in or near the active sites of the enzyme, while serine and lysine were indirectly involved in the enzymic activity. The intracellular cytosine deaminase from C violaceum YK 391 was assumed to be a thiol enzyme.