• Title/Summary/Keyword: Chloramine

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Preparation of Radiopharmaceuticals-(1) (방사성(放射性) 의약품(醫藥品) 합성방식(合成方式)에 관(關)한 연구(硏究) -제 1 부-(第 1 報))

  • Kim, You-Sun;Kim, Soon-Ok;Kim, Chong-Doo
    • The Korean Journal of Nuclear Medicine
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    • v.1 no.1
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    • pp.83-87
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    • 1967
  • The iodine containing radiopharmaceuticals, Hippuran, L-Thyroxine, Triiodothyronine, Rose Bengal, RISA, MAA, Triolein, Oleic acid and sterilized iodide solution were prepared. The labelling yield was av. 100-70%. The exchange method, iodination method, and chloramine-T procedure for a low temperature iodination were adopted as the preparative procedures. The preparative procedures and pyrogen free test of products were described and the distribution activity of the products in this institute was reported.

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Enzymatic Radioiodination of Insulin for Radioimmunoassay Use

  • Awh, Ok-Doo;Kim, Jae-Rok
    • Nuclear Engineering and Technology
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    • v.12 no.2
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    • pp.81-87
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    • 1980
  • Insulin was labelled with $^{125}$ I using lactoperoxidase as an oxidizing agent. The reaction product was purified via two stages: a starch gel electrophoresis(SGE) and a Sephadex gel filtration (SF). Upon comparison of the labelling yields and the bindabilities of the labelled insulin to its antibody, it has been found that the enzyme method shows higher yields (50%) and the better bindability to its antibody than the conventional chloramine-T method (35%). By checking the insulin blank labelling mixture with a SGE, a paper chromatography, and a radioautography technique, a by-product in the lactoperoxidase method has been identified. The separated fractions in SGE and SF were also analyzed and discussed.

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$^{125}I$ Labelling of Protein Using Immobilized Enzyme (고정화효소에 의한 단백질의 $^{125}I$ 표지반응)

  • Kim, Jae-Rok;Park, Kyung-Bae;Awh, Ok-Doo
    • The Korean Journal of Nuclear Medicine
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    • v.18 no.1
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    • pp.55-62
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    • 1984
  • For an effective solid-phase labelling of protein with $^{125}I$, studies on the immobilization of lactoperoxidase(LPO) on the inner wall of polystyrene tubes were carried out. Labelling of bovine serum albumin(BSA) and insulin was also practiced using the LPO immobilized tubes. The immobilized enzyme of about $2.5{\mu}g/tube$ was sufficient for small scale labelling since the results of radio-paper chromatography of the labelling mixture of insulin indicated that the yields were sufficiently high(80%) even in the reactions conducted at room temperature for 60 sec. The results of the Sephadex column chromatography indicated that the labelled products were not contaminated with $LPO-^{125}I$, and the radiochemical purity of the products was more than 90%. In considering the general trend that the $^{125}I$ labelled protein obtained by using LPO maintains its intactness better than those obtained by using chloramine-T, together with the tendency of yield enhancing with increase of reactants-concentration, the LPO immobilized tube method is estimated to be one of the simple methods of labelling. The product might be applicable without further purification.

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Chemical Modification of Extracellular Cytosine Deaminase from Chromobacterium violaceum YK 391

  • Kim, Tae-Hyun;Yu, Tae-Shick
    • Journal of Microbiology and Biotechnology
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    • v.8 no.6
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    • pp.581-587
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    • 1998
  • Essential amino acids involved in the catalytic role of the extracellular cytosine deaminase from Chromobacterium violaceum YK 391 were determined by chemical modification studies. The enzyme activity required the reduced form of Fe (II) ion, since the enzyme was inhibited by ο-phenanthroline. The enzyme activity was completely inhibited by the chemical modifiers, such as p-chloromercuribenzoate (p-CMB), p-hydroxymercuribenzoate, and chloramine-T at 1 mM each. The enzyme activity was also markedly inhibited by pyridoxal-5'-phosphate, diethyl pyrocarbonate, and phenylmethylsulfonyl fluroride at 1 mM each. The inactivation of the enzyme activity with p-CMB was reversed by a high concentration of cytosine. Furthermore, the inactivation of the enzyme activity with p-CMB was also reactivated by 1 mM dithiothreitol, 1 mM 2-mercaptoethanol, 1 mM cysteine-HCI, 10% ethyl alcohol, and 10% methyl alcohol. These results suggested that cysteine and methionine residues might be located in or near the active site of the enzyme, while lysine, histidine, and serine residues might be indirectly involved in the enzyme activity.

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Radio Iodination of Organic Compounds (1) A Low Temperature Procedures (放射性 沃化反應 (第 1 報) 低溫沃化反應)

  • YOU SUN KIM;CHONG DOO KIM
    • Journal of the Korean Chemical Society
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    • v.11 no.2
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    • pp.51-55
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    • 1967
  • A procedure, which is effective enough to label various compounds at low temperature by radioactive iodine, was investigated. The chloramine-T procedure was mostly effective for labelling various protein, amino acids, hormones, and organic compounds by iodine, and the procedure was able to afford both high specific activity and high radiochemical yield. However, the procedure was ineffective for labelling unsaturated compounds or other organic compounds which has not active aromatic nucleus of reactive character. The radiochemical yield of the procedure was generally averaged from 100% to 60%. The reactivity of the aromatic part of the organic compound towards this reagent was correspond to that of an electrophillic reagent. The procedures were described and the reaction path was considered.

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Kinetic and Mechanistic Studies of Oxidation of an Antiallergic Drug with Bromamine-T in Acid and Alkaline Media

  • Puttaswamy, Puttaswamy;Sukhdev, Anu
    • Bulletin of the Korean Chemical Society
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    • v.33 no.11
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    • pp.3544-3550
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    • 2012
  • Cetrizine dihydrochloride (CTZH) is widely used as an anti-allergic drug. Sodium N-bromo-p-toluenesulfonamide or bromamine-T (BAT) is the bromine analogue of chloramine-T (CAT) and is found to be a better oxidizing agent than CAT. In the present research, the kinetics of oxidation of CTZH with BAT in acid and alkaline media was studied at 313 K. The experimental rate laws obtained are: -d[BAT]/dt=$k[BAT][CTZH]^{0.80}[H^+]^{-0.48}$ in acid medium and -d[BAT]/dt=$k[BAT][CTZH]^{0.48}[OH^-]^{0.52}[PTS]^{-0.40}$ in alkaline medium where PTS is p-toluenesulfonamide. Activation parameters and reaction constants were evaluated. The solvent isotope effect was studied using $D_2O$. The dielectric effect is positive. The stoichiometry of the reaction was found to be 1:1 and the oxidation products were identified as 4-chlorobenzophenone and (2-piperazin-1-yl-ethoxy)-acetic acid in both media. The rate of oxidation of CTZH is faster in acid medium. Suitable mechanisms and related rate laws have been worked out.

Change of hCG Binding Capacity on the Granulosa Cell of Porcine Ovary During Follicular Atresia (돼지 난소내 여포의 폐쇄과정중 과립세포의 결합능의 변화)

  • Chang, Choul-Soo;Lee, Chang-Joo;Yoon, Yong-DaI;Kim, Moon-Kyoo
    • Clinical and Experimental Reproductive Medicine
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    • v.13 no.1
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    • pp.29-38
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    • 1986
  • In order to study the mechanism of follicular atresia, follicles were classified into the normal groups and the atretic ones, according to the criteria with or without corpus luteum, size of follicles, vascularization, status of granulose cells and the hypertrophy of theca layers in the porcine ovary. To estimate the binding capacity of human chorionic gonadotropin (hCG) receptor on the granulosa cells during atresia, hCG were iodinated by the chloramine-T method and then purified through the column chromatography. The concentration" of hCG receptor in each group were measured by the hCG receptor binding assay. Binding capacity in large normal follicles were 1.16%, but atretic ones were 0.45%. But in medium and small follicles (below 6mm in diameter), the binding capacity in normal follicles were 0.09%, but atretic ones were 0.05%, which was lower than those of large follicles. The present ( ) that the concentrations of hCG receptors on granulosa cells is decreased when the follicles become atretic and be used as a sort of creteria for the identification of follicles atresia.

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Preparation of Radioiodine Labelled Human Follicle Stimulating Hormone for Radioimmunoassay Use

  • Kim, Jae-Rok;Kim, Tae-Ho;Kim, You-Sun
    • The Korean Journal of Nuclear Medicine
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    • v.11 no.1
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    • pp.9-15
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    • 1977
  • Radioiodine labelled human follicle stimulating hormone has been prepared using chloramine-T, with the approximate labelling yield of 65%. The labelled product is purified by means of a starch gel electrophoresis, and a Sephadex gel filtration, and the separation efficiencies are assessed for the effective use in radioimmunoassay. The results indicate that the gel filtration is efficient in view of the separation time, simplicity and bindability of the labelled hormone to the antibody. In determining the ratio of the free to the antibody hound labelled hormone, a double antibody technique is applied in comparison with a chromatoelectrophoresis. The ratio could be obtained only in the case of applying the double antibody technique.

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Synthesis of 125I-labeled thiol-reactive prosthetic group for site-specific radiolabeling of human serum albumin

  • Shim, Ha Eun;Song, Lee;Jeon, Jongho
    • Journal of Radiopharmaceuticals and Molecular Probes
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    • v.4 no.2
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    • pp.85-89
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    • 2018
  • We demonstrate a detail protocol for the radiosynthesis of an $^{125}I$-labeled MSTP prosthetic group and its application to the efficient radiolabeling of human serum albumin (HSA). Radioiodination of the 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 MSTP ($[^{125}I]1$) was obtained with high radiochemical yield ($73{\pm}5%$, n = 3) and excellent radiochemical purity (>99%). Site-specific reaction between ($[^{125}I]1$) and HSA gave the $^{125}I$-labeled human serum albumin ($[^{125}I]3$) with more than 99% of radiochemical yield as determined by radio-thin-layer chromatography (radio-TLC). These results clearly demonstrate that the present radiolabeling method will be useful for the efficient and convenient radiolabeling of thiol-bearing biomolecules.

Study on radiolabeling method of chitosan to improve the radiolabeling yield of the final product

  • Jung Ae Kang;A-Ram Yu;Jae Jun Lee;Yeong Su Ha
    • Journal of Radiopharmaceuticals and Molecular Probes
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    • v.7 no.2
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    • pp.113-118
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    • 2021
  • Chitosan is a polysaccharide derived from chitin by deacetylation. Chitosan is non-toxic, biodegradable, and biocompatible, so that it can be used in wide variety of medical applications such as wound healing and antimicrobial biomaterials. It also used as dermal fillers due to its ability to inject with liquid formulations. For investigation on in vivo distribution of these chitosans, Bolton-Hunter-conjugated chitosan (Chitosan-BH) was synthesized by the reaction between the primary amino group of chitosan and N-hydroxysuccinimide ester group of Bolton-Hunter reagent. Then Chitosan-BH was radiolabeled with 125I (Chitosan-BH-125I) using a Chloramine-T method. The effects of each radiolabeling step on the radiolabeling yield of the final product were tested. The results showed that purification step had significant effects on the radiolabeling yield of the final product. Finally, SPECT/CT images were obtained to evaluate in vivo uptake of the radiolabeled chitosan (Chitosan-BH-125I) in several organs. The highest uptake was found in the site of injection at 21 days post-injection. The results of this study suggest that chitosan is expected to be useful for biomaterials of dermal fillers.