• YAKHAK HOEJI
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• v.16 no.4
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• pp.180-185
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• 1972

A new spectrophotometric method was established for the determination of undecylenic acid. The method is based on the solvent extraction into nitrobenzene of the ion pair formed between tris(1,10-phenanthroline)Fe(II) chelate and the anion of undecylenic acid. The maximum absorbance of the extract in the organic phase was at 518nm. A maximum extraction was obtained at pH 9-11, when excess of at least 50-fold(molar) of the phenanthroline-Fe(II) chelate to undecylenic acid was present. The color intensity of the extracted species remained constant at room temperature for the several hours after separation of the organic layer. A linear relationship was obtained over the tested range of 5-20${\gamma}$/ml of undecylenic acid. The effect of several other fungicids on this method was investigated. The method was applied to the determination of undecylenic acid in preparations and the results were in good agreement with those added amounts.

• YAKHAK HOEJI
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• v.45 no.1
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• pp.29-33
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• 2001

A method for the determination of anionic drug, mefenamate with ion-selective electrode using Fe(II)-1,10-phenanthroline chelate as a counter ion was developed. Benzyl nitrophenyl ether (BNPE) plasticized membrane was more selective and sensitive than the other tested membranes. This membrane electrode exhibits a linear response for 10$^{-2}$ M~5 $\times$ 10$^{-5}$ M of mefenamic acid with a slope of -61.4 mV/dec. in borate buffer solutions (pH 9.0). Potentiometric selectivity measurements revealed negligible interferences from various organic and ionorganic anions. Direct potentiometry and potentiometric titration method of mefenamic acid in capsule preparations are presented and compared.

• Bulletin of the Korean Chemical Society
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• v.23 no.3
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• pp.399-403
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• 2002

The complex of iron(II) tris(3-Br-phen) (3-Br-phen; 3-bromo-1,10-phenanthroline) was prepared as a precursor of electropolymerization and the crystal structure of [Fe(3-Br-phen)3]($PF_6$)2${\cdot}$CH3CN with a distorted octahedral geometry has been investigated. The reductive electropolymerization of $>[Fe(3-Br-phen)3]^{2+}$ complex onto the surface of a glassy carbon electrode and indium tin oxide (ITO) optically transparent electrode were performed in acetonitrile at room temperature. Thin film of poly-$>[Fe(3-Br-phen)3]^{2+}$ formed was adherent, electroactive and stably deposited on a glassy carbon disk electrode. The thin metallopolymeric film formed was also confirmed by absorption spectroscopy.

• Biomedical Science Letters
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• v.6 no.4
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• pp.261-268
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• 2000

Fibrinolytic enzyme (FE-2) was purified from the fruiting bodies of Tricholoma saponaceum using DEAE-Cellulose chromatography and Mono-S column chromatography, The enzyme has a molecular weight of 18.23 kDa and include Zn$^{2+}$ ion as found by ICP/MS. The N-terminal amino acid sequence of the enzyme was A-L-Y-V-G-X-S-P-X-Q-Q-S-L-L-V It has a pH optimum at pH 7.5, suggested that FE-2 was a neutral pretense. The activity of FE-2 was highly inhibited by EDTA and 1,10-phenanthroline, indicating that the enzyme is a metalloprotease. The activity of FE-2 was increased by $Mg^{2+}$, Zn$^{2+}$, Fe$^{2+}$, and Co$^{2+}$, but the enzyme activity was totally inhibited by Hg$^{2+}$. No inhibition was found with PMSF, E-64, pepstatin and 2-mercaptoethanol. The enzyme hydrolyzed both $A\alpha$ and B$\beta$ chains of human fibrinogen. The $\gamma$ chain was resistant to hydrolysis by FE-2.

• Korean Journal of Plant Resources
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• v.11 no.2
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• pp.195-201
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• 1998

Some morphological character were surveyed and PR-proteinases were induced and characterized from Lilium formosanum Wallace endeimc to Cheju island . Its flower characters were similar to those of white trumpet lilies(Lilium longiflorum Thunb) although its flowering period was later than that of white trumpet lilies and it hadd a wide range of variation among individuals. Six PR-proteinases(II-2, III-1, III-2, IV-1, IV-2 and V) were induced from bulbs by 2.5mM salicylic acid and almost excreted into the intercellular spaces. These PR-proteinases were strongly activated by Ca 2+, , whereas they were strongly inhibited by Cu2+ Co2+ and Fe2+ . Three PR proteinases(II-2, IV-1 and IV-2) were strongly inhibited by 1, 10 -phenanthroline, indicating that these enzymes are metallo-proteinases. Three PR-proteinases(III-1, III-2 and V) had a high sensitivity to PMSF and required $\beta$-mercaptoethanol for their activities. These results indicate that these proteinases are cysteine proteinases.

• 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.