• Journal of the Korean Chemical Society
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• v.33 no.5
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• pp.452-458
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• 1989

The crystal structures of vacuum-dehydrated $Ag^+\;and\;Ca^{2+}$ exchanged zeolite A, Ag_7Ca_{2.5}-A(a = 12.310(1){\AA})$ and $Ag_2Ca_5-A(a = 12.287(2){\AA})$ have been determined by single-crystal X-ray diffraction methods in the cubic space group Pm3m at $21(1)^{\circ}C$. The crystals of $A_7Ca_{2.5}-A\;and\;Ag_2Ca_5-A$ were prepared by flow method using exchange solutions in which mole ratios of $AgNO_3\;and\;Ca(NO_3)_2$ were 1:50 and 1:1000, respectively, with total concentration of 0.05 M. Full-matrix least-squares refinement converged to the final error indices of R1 = 0.056 and R2 = 0.059 for $Ag7Ca2.5-A$, and R1 = 0.054 and R2 = 0.082 for $Ag2Ca5-A$ using 306 and 348 reflections, respectively, for which I >3 {\sigma}$ (I). 5.5 $Ag^+$ ions and 2.5 Ca^{2+}$ ions for $Ag_7Ca_{2.5}-A\;and\;2\;Ag^+$ ions and 5 $Ca^{2+}$ ions for $Ag_2Ca_5-A$ lie on two crystallographically nonequivalent threefold axes on the 6-rings. Both structures indicate that smaller Ca2+ ions preferentially occupy 6-ring sites and larger $Ag+$ ions occupy 8-ring sites when total number of cations per unit cell is more than 8.

• Journal of the Korean Chemical Society
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• v.32 no.6
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• pp.520-527
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• 1988

The crystal structures of $Co^{2+}\;and\;Ag^+\;exchanged\;zeolite\; A,\; Ag_6Co_3$-A(a = 12.131(5)$\AA$) and $Ag_3Co_{4.5}$-A(a = 12.145(1)$\AA$), have been determined by single crystal X-ray diffraction techniques. Both structures were solved and refined in the cubic space group Pm3m at 21(1)$^{\circ}C$. Full-matrix leastsquares refinement converged to the final error indices of R1 = 0.045 and R2 = 0.041 for $Ag_3Co_{4.5}-A,\; and\; R1 = 0.066\; and\; R2 = 0.076\; for\; Ag_6Co_3$-A using the 258 and 189 reflections, respectively, for which I > 3$\sigma$(I). Both structures indicate that CO(Ⅱ)ions are coordinated by three framework oxygens; the Co(II) to O(3) distances are 2.118(4)$\AA$ for $Ag_3Co_{4.5}$-A and 2.106(1)$\AA$ for $Ag_6Co_3-A$, respectively. In each structure, the angle substended at Co(II), O(3)-Co(II)-O(3) is ca 120°, close to the idealized trigonalplanar value. $Co^{2+}$ ions prefer to 6-ring sites and $Ag^+$ ions prefer to 8-ring site when total number of cations is more than 8. The crystals of hydrated and dehydrated $Ag_{12-2x}Co_x-A (x > 4.5)$ had no crystalline diffraction pattern, indicating the apparent exchange limit of $Co^{2+}\; into\; Ag_{12}-A\; is\; 4.5 Co^{2+}$ ions per unit cell. $Co^{2+}$ ions hydrolyze $H_2O$ molecules and $H_3O^+$ concentraction is accumulating. These $H_3O^+$ ions destroy the zeolite structures.

• Korean Journal of Crystallography
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• v.15 no.2
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• pp.59-68
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• 2004

Three crystal structures of dehydrated partially $Co^{2+}-exchanged$ zeolite A treated with 0.6 Torr of K at $300^{\circ}C$ (for 12 hrs, 6 hrs, and 2 hrs) vapor have been determined by single-crystal X-ray diffraction techniques in the cubic space group Pm3m at 21(1)$^{\circ}C(a=12.181(1)\;{\AA},\;a=12.184(1)\;{\AA},\;and\;a=12.215(1)\;{\AA})\;respectively)$. Their structures were refined to the final error indices, R(weight) of 0.090 with 10 reflections, 0.091 with 82 reflections, and 0.090 with 80 reflections, respectively, for which $1>\sigma(I)$. In each structure, all four $Co^{2+}$ and four $Na^+$ ions to be reduced by K atoms. The cobalt and sodium atoms produced are no longer found in the zeolite. K species are found at five different crystallographic sites: three $K^+$ ions lie at the planes of 8-rings, filling that position, ca. 11.5 K^+$ ions lie on threefold axes, ca. 4.0 in the large cavity and ca. 4.0 in the sodalite cavity, and ca. 0.5 $K^+$ ion is found near a 4-ring. ca. three $K^0$ atoms are found deep into the large cavity on threefold axes. In these structures, crystallographic results show that cationic tetrahedral $K_4$ (and/or triangular $K_3$) clusters have formed in the sodalites of zeolite A. The $K_4$ and/or $K_3$ clusters coordinate trigonally to three oxygens of a six-oxygen ring. The partially reduced ions of these clusters interact primarily with oxygen atoms of the zeolite structure rather than with each other. ca. 14.5K species are found per unit cell, more than the twelve $K^+$ ions needed to balance the anionic charge of zeolite framework, indicating that sorption of $K^0$ has occurred. The three $K^0$ atoms in the large cavity are closely associated with three out of four $K^+$ ions in the large cavity to form $K_7^{4+}$ clusters. The $K_7^{4+}$ cluster not interacts primarily with framework oxygens.

• Korean Journal of Crystallography
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• v.6 no.2
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• pp.125-133
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• 1995

The crystal structure of dehydrated, partially Co(II)-exchanged zeolite X, stoichiometry Co2+Na+-X (Co41+Na10Si100Al92O384) per unit cell, has been determined from three-dimensional X-ray diffraction data gathered by counter methods. The structure was solved and refined in the cubic space group Fd3:α=24.544(1)Å at 21(1)℃. The crystal was prepared by ion exchange in a flowing stream using a solution 0.025 M each in Co(NO3)2 and Co(O2CCH3)2. The crystal was then dehydrated at 380℃ and 2×10-6 Torr for two days. The structure was refined to the final error indices, R1=0.059 and R2=0.046 with 211 reflections for which I > 3σ(I). Co2+ ions and Na+ ions are located at the four different crystallographic sites. Co2+ ions are located at two different sites of high occupancies. Sixteen Co2+ ions are located at the center of the double six-ring (site I; Co-O = 2.21(1)Å, O-Co-O = 90.0(4)°) and twenty-five Co2+ ions are located at site II in the supercage. Twenty-five Co2+ ions are recessed 0.09Å into the supercage from its three oxygen plane (Co-O = 2.05(1)Å, O-Co-O = 119.8(7)°). Na+ ions are located at two different sites of occupandies. Seven Na+ ions are located at site II in the supercage (Na-O = 2.29(1)Å, O-Na-O = 102(1)°). Three Na+ ions are statistically distribyted over site III, a 48-fold equipoint in the supercages on twofold axes (Na-O = 2.59(10)Å, O-Na-O = 69.0(3)°). Seven Na+ ions are recessed 1.02Å into the supercage from the three oxygen plane. It appears that Co2+ ions prefer sites I and II in order, and that Na+ ions occupy the remaining sites, II and III.

• Korean Journal of Veterinary Research
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• v.25 no.1
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• pp.7-17
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• 1985

Many investigators have been pursuing various attempts so far to produce hepatitis B surface antigen(HBsAg) vaccines using the techniques such as isolation from plasma of chronic HBsAg carrier, recombinant DNA technique or preparation of synthetic peptides specific for immunogenic determinants. Hepatitis B virus can not grow on any cell lines by the tissue culture technique at the present time. The plasma of chronic HBsAg carrier is expensive and its source is limited. The HBsAg from the recombinant DNA technique gave still very low yield. Another approach, therefore, has been initiated to develop a synthetic hepatitis B virus vaccine. The possible use of several distinct synthetic vaccines in prophylaxis can be facilitated by availability of full synthetic immunogens. Peptides synthesized for potential application as antiviral vaccines have been mostly tested in the form of conjugates with carrier proteins, although the free synthetic peptide can be immunogenic. To understand basic knowledges on the antigenicity and immunogenicity of a synthetic peptide specific for major immunogenic determinant of HBsAg, a nonapeptide, $H_2N^{139}Cys-Thr-Lys-Pro-Thr-Asp-Gly-^{146}Asn-Aba$ COOH, which corresponds to HBsAg amino acid residues 139 to 147, was synthesized by the Merrifield's solid-phase method with a slight modification. The antigenicity and immunogenicity of this specific synthetic peptide were examined comparing with purified plasma-derived natural HBsAg. The results obtained are as follows; 1. The peptide synthesized showed the identical amino acid composition to the theoretical value. The degree of purification and molecular weight were acertained by methods of high performance liquid chromatography and mass spectrometry. 2. Using m-maleimidobenzoyl-N-hydroxysuccinimide ester as a conjugating agent, the synthetic peptide was conjugated to rabbit albumin and ${\gamma}$-globulin, tetanus and diphtheria toxoids, and keyhole limpet hemocyanin. Their conjugation yields were 8.3, 9.5, 15.8, 13.5, and 11.2%, respectively. 3. The natural HBsAg was purified from plasma of chronic HBsAg carrier. By the electron microscopic observation of the purified natural HBsAg preparation, no Dane particles were observed and the preparation showed negative DNA polymerase activity. 4. Antigenicity of the synthetic peptide and the plasma-derived natural HBsAg was determined by competition radioimmunoassay using $^{125}I$-natural HBsAg. Their 50% inhibitions appeared as $90{\mu}g/ml$ and $0.12{\mu}g/ml$ for the synthetic peptide and the natural HBsAg, respectively. This indicates that the former was about 750-fold less antigenic than the latter. 5. Immunogenicity of the synthetic peptide was determined by administering the peptide-carrier conjugates into rabbits with and without Freund's complete adjuvant. Regardless the carrier proteins and adjuvant, positive immune responses to the synthetic peptide were observed. The higher antibody titers, however, were shown in the groups administered with Freund's complete adjuvant. 6. Immunizing dose 50% in mice of the various peptide-carrier conjugates was 5.47, 6.00, 65.16, 31.25 and $13.03{\mu}g/dose$ for rabbit albumin and ${\gamma}$-globulin, tetanus and diphtheria toxoids, and keyhole limpet hemocyanin, respectively, while the natural HBsAg showed $0.65{\mu}g/dose$. 7. It was postulated that homologous proteins prefer to heterologous ones as the carriers.

• Korean Journal of Microbiology
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• v.38 no.3
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• pp.153-161
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• 2002

Sox4, a transcription factor, consists of three functional domains: an HMG-box domain as a DNA binding domain, serine rich region as a transactivation domain and glycine rich region (GRR), an unknown functional domain. Although Sox4 is known to be functionally involved in heart, B-cell and reproductive system development, its physiological function remains to be elucidated. We used pGEX expression system to develop a simple and rapid method for purifying Sox4 protein in suitable forms for biochemical studies of their functions. Unexpectedly, we observed that full-length Sox4 appears to be protease-sensitive during expression and purification in E. coli. To map the protease-sensitive site in Sox4, we generated various constructs with each of functional domains of Sox4 and purified as the GST-Sox4 fusion proteins using glutathione beads. We found that the specific cleavage site for the proteolytic enzyme, which exists in E. coli, is localized within the novel GRR of Sox4. Our study suggest that the GRR of Sox4 may a target for the cellular protease action and this cleavage in the GRR may be involved in regulating physiological function of Sox4. Additionally, our study may provide a useful method for investigating the proteolytic cleavage of the target molecule in E. coli.

• Journal of Korean Port Research
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• v.6 no.2
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• pp.65-92
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• 1992

The Korean central government has not appreciate the full extent of the impact of seaports on the national economy. As a consequence port investment has not been given sufficient priority and capacity has failed to keep pace with demand. The principal reason for this failure is the fact that the linkages (or relationships) of the port transport industry with other sectors have not been quantified and fully appreciated. To overcome this dificiency this paper developed a port input-output model to determine the economic impact of the port industry on the national economy. This impact study was conducted by analysing the impact of the Korean port industry upon the national economy from the macroeconomic viewpoint, and identifying the spreading effects of port investments upon the nation's economy. The analysis of the economic impact of the port industry suggests that its contribution to the Korean economy is substantial. What the model shows is, in quantifiable terms, there are the strong economic linkages between the port industry and the other sectors of the national economy. The contribution of the port industry to the Korean economy was summarised in the Conclusion section.

• The Korean Journal of Nuclear Medicine Technology
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• v.25 no.1
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• pp.34-40
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• 2021

Purpose If a new test is introduced or reagents are changed in the laboratory of a medical institution, the characteristics of the test should be analyzed according to the procedure and the assessment of reagents should be made. However, several necessary conditions must be met to perform all required comparative evaluations, first enough samples should be prepared for each test, and secondly, various reagents applicable to the comparative evaluations must be supplied. Even if enough comparative evaluations have been done, there is a limit to the fact that the data variation for the new reagent represents the overall patient data variation, The fact puts a burden on the laboratory to the change the reagent. Due to these various difficulties, reagent changes in the laboratory are limited. In order to introduce a competitive bid, the institute conducted a full investigation of Radioimmunoassay(RIA) reagents for each test and established the range of reagents available in the laboratory through comparative evaluations. We wanted to share this process. Materials and Methods There are 20 items of tests conducted in our laboratory except for consignment tests. For each test, RIA reagents that can be used were fully investigated with the reference to external quality control report. and the manuals for each reagent were obtained. Each reagent was checked for the manual to check the test method, Incubation time, sample volume needed for the test. After that, the primary selection was made according to whether it was available in this laboratory. The primary selected reagents were supplied with 2kits based on 100tests, and the data correlation test, sensitivity measurement, recovery rate measurement, and dilution test were conducted. The secondary selection was performed according to the results of the comparative evaluation. The reagents that passed the primary and secondary selections were submitted to the competitive bidding list. In the case of reagent is designated as a singular, we submitted a explanatory statement with the data obtained during the primary and secondary selection processes. Results Excluded from the primary selection was the case where TAT was expected to be delayed at the moment, and it was impossible to apply to our equipment due to the large volume of reagents used during the test. In the primary selection, there were five items which only one reagent was available.(squamous cell carcinoma Ag(SCC Ag), β-human chorionic gonadotropin(β-HCG), vitamin B12, folate, free testosterone), two reagents were available(CA19-9, CA125, CA72-4, ferritin, thyroglobulin antibody(TG Ab), microsomal antibody(Mic Ab), thyroid stimulating hormone-receptor-antibody(TSH-R-Ab), calcitonin), three reagents were available (triiodothyronine(T3), Tree T3, Free T4, TSH, intact parathyroid hormone(intact PTH)) and four reagents were available are carcinoembryonic antigen(CEA), TG. In the secondary selection, there were eight items which only one reagent was available.(ferritin, TG, CA19-9, SCC, β-HCG, vitaminB12, folate, free testosterone), two reagents were available(TG Ab, Mic Ab, TSH-R-Ab, CA125, CA72-4, intact PTH, calcitonin), three reagents were available(T3, Tree T3, Free T4, TSH, CEA). Reasons excluded from the secondary selection were the lack of reagent supply for comparative evaluations, the problems with data reproducibility, and the inability to accept data variations. The most problematic part of comparative evaluations was sample collection. It didn't matter if the number of samples requested was large and the capacity needed for the test was small. It was difficult to collect various concentration samples in the case of a small number of tests(100 cases per month or less), and it was difficult to conduct a recovery rate test in the case of a relatively large volume of samples required for a single test(more than 100 uL). In addition, the lack of dilution solution or standard zero material for sensitivity measurement or dilution tests was one of the problems. Conclusion Comparative evaluation for changing test reagents require appropriate preparation time to collect diverse and sufficient samples. In addition, setting the total sample volume and reagent volume range required for comparative evaluations, depending on the sample volume and reagent volume required for one test, will reduce the burden of sample collection and planning for each comparative evaluation.

• Parasites, Hosts and Diseases
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• v.27 no.4
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• pp.231-248
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• 1989

The growth and development of the metacercariae of F. seoulensis cultivated in vitro or on the chick chorioallantois were assessed by comparison with the optimum process of maturation in albino rats and new born chickens. The process of maturation was divided for convenience into six stages: Stage 1 ; cell multiplication, Stage 2; body shaping, Stage 3; separation of genital anlagen, Stage :1 organogeny, Stage 5; gametogony, and Stage 6: oviposition. In Hank's and Tyrode's .solutions, the metacercariae were alive up to 200 days or more at $4^{\circ}C$ without any development. The in vivo maturation process in rats or chicks was as follows: stage 1 from 6 hours; stage 2 from 24 hours; stage 3 from 48 to 72 hours; stage 4 from 3 to 4 days; stage 5 from 4 to 5 days; and stage 6 from 5 to 8 days. Despite unsuccessful infection of the metacercariae to 12 day old chicks, fully mature worms of stage 5 or 6 were recovered from new born chicks (1 to 2 days old), The metacercariae of F. seoulensis grown in vitro were up to stage 3 and no further maturation was observed. Of various media employed, the medium NCTC 109 (Gibco) or NCTC 135(Gibco) supplemented with 20% egg yolk or 20% whole egg macerate or 0.5% yeast was basically required for the earlier development of the fluke. It took 16.1 days(in average) to reach the stage 3 after cultivation. The metacercariae cultivated on the chorioallantoic membranes of 6∼13 day old chick embryo at 37∼38℃ showed their full development up to stage 5 or 6. However, the worms were in general remarkably retarded, compared with those grown in rats or chickens. In the experiments of worm transplant, although the transfer was failed from in vitro culture to in vivo of rats(Per os), the transplants from in vitro culture to the chorioallantois and from the choriollantois to in vivo of rat host were successful with or without development of the transferred worms. In the present study, it was observed that the metacercariae of F, seoulensis can be maintained in vitro media with poor development as well as fully matured in 1 to 2 day-old chicks or on the chorioallantois at a very low rate.