• Proceedings of the Korean Society of Toxicology Conference
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• 2003.05a
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• pp.88-88
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• 2003

n view of the role of haptoglobin as a candidate for physical performance, we investigated the protein polymorphism of the haptoglobin in elite Korean male athletes. The serum sample was collected from 120 Korean male eliteathletes. The haptoglobin phenotypes were determined by polyacrylamide gel electrophoresis, followed by peroxidase staining. (omitted)

• The Korean Journal of Malacology
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• v.12 no.1
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• pp.39-45
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• 1996

Polyacrylamide gel electrophoresis was used to reveal the esterase isozyme patterns of a freshwater snail, Semisulcospira gottschei, in the lake Uiam. From the result with inhibitors, it is tentatively concluded that four types (arylesterase, carboxylesterase, acethylesterase, acethylcholinesterase)of the adult(means of allele per locus=1.16, %polymorphism=16.7, heterozygosity=0.082)was lower than the juveniles(A=1.7, %P=16.7, H$\sub$D/=0.2215).

• The Korean Journal of Zoology
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• v.15 no.2
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• pp.92-93
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• 1972

Ox-RBC로부터 Moddy法에 依하여 Ox-RCM抗原을 抽出하여 몇가지 分析을 實施하였다. Lyophilized 한 Ox-RCM protein의 化學的 分析 結果 total protein은 $55\\pm 1.3%$, total nitrogen은 9.2%, carbohydrate 8.5% 그리고 total acid soluble phosphorus는 $0.96\\pm 0.1%$였다. Polyacrylamide gel electrophoresis한 結果 Ox-RCM은 12 $\\sim$ 15個, Pre-VRS fraction은 8個 및 PHR 分劃은 9個의 pattern을 나타냈다. Amino acid의 分析 結果로 cystine이 4.93 $\\sim$ 3.72 moles/100 moles 이고 glycine이 最高로 26.7 $\\sim$ 13.5 moles/100 moles였고 最低로 methionine 이었으나 試料의 抽出方法에 따라 그 値의 變動을 볼 수 있다.

• Korean Journal of Food Science and Technology
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• v.23 no.4
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• pp.394-399
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• 1991

The strain OK-63 isolated from katsuobushi was cultured on wheat bran medium and the isolate was morphologically identified as an Aspergillus niger group and showed maximum pretense activity and multiplication after 6 days of cultivation. Protease was purified by ammonium sulfate fractionation. Sephadex G-100 gel filtration and DEAE-cellulose column chromatography. The purified enzyme showed single band by polyacrylamide gel electrophoresis and the purity was 150 times higer than crude enzyme. The recovery of enzyme activity was found to be 45%.

• Journal of Microbiology and Biotechnology
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• v.6 no.6
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• pp.402-406
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• 1996

Inulin fructotransferase (depolymerizing) (EC 2.4.1.93) was purified 34-fold from the culture broth of Arthrobacter sp. A-6 by using a combination of ammonium sulfate fractionation, DEAE-Sepharose CL-6B chromatography and Sephacryl S-200 gel filtration. The purified enzyme converts inulin into di-D-fructofuranose dianhydride III(DFA III) and small quantities of fructo-oligosaccharides. The temperature and pH optima of the enzyme were $70^{\circ}C$ and 6.0, respectively. Molecular weight of the enzyme was determined to be 49 kDa by 12$%$ SDS-polyacrylamide gel electrophoresis, and 145 kDa by Sephacryl S-200gel filtration. This indicates that the functional inulin fructotransferase of Arthrobacter sp. A-6 has a homomeric trimer structure. The enzyme had an isoelectric point of pH 4.6. The N-terminal amino acid sequence of the purified enzyme subunit was Ala-Asp-Asn-Pro-Asp-Gly(\ulcorner)-Ser-Asn-Met(or Glu)-Tyr-Asp-Val.

• Korean Journal Plant Pathology
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• v.11 no.4
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• pp.312-317
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• 1995

The polygalacturonase (PG) production in rotten apples by Botryosphaeria dothidea was purified by using gel filtration and ion exchange column chromatography, and the biochemical characters of PG were investigated. The purified PG appeared as a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) with approximate molecular weight of 49 kilodalton (kDa). The molecular weight was equal to the native molecular weight estimated by gel filtration. The Km and Vmax values of PG were 0.51 mg/ml and 90.9 $\mu$M/min/ml, respectively. Optimum pH was 4.0~5.0, and the PG activity was stable from pH 5.0~10.0. Optimum temperature of the enzyme activity was 4$0^{\circ}C$. The PG activity was relatively stable at 2$0^{\circ}C$, but it was reduced 45% at 4$0^{\circ}C$ and completely inactivated at 8$0^{\circ}C$. The PG activity was considerably inhibited by Cu2+, Zn2+, SDS and EDTA, whereas it was not effected by Ca2+, K+, Mg2+ or Na+ ions.

• Journal of Microbiology and Biotechnology
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• v.8 no.1
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• pp.92-95
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• 1998

Overproduction of Escherichia coli thiol peroxidase in the periplasmic space was achieved by locating the appropriate gene on a downstream region of the strong T7 promoter. E. coli strain BL21 carrying the recombinant plasmid pSK-TPX was induced by IPTG, lysed, and analyzed by SDS-polyacrylamide gel electrophoresis. A large amount of the overexpressed thiol peroxidase was located in the periplasmic space. A homogeneous thiol peroxidase was obtained from E. coli osmotic shock fluid by simple one-step gel permeation chromatography.

• Microbiology and Biotechnology Letters
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• v.17 no.6
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• pp.587-592
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• 1989

A strain of alkalophilic Bacillus sp. YS-309 capable of producing large amount of $\beta$-galactosidase has been isolated from soil sample. Intracellular $\beta$-galactosidase was purified 6.9 folds by procedures including ammonium sulfate precipitation, DEAE-cellulose chromatography, gel-filtration, DEAE-Sephadex A-50 chromatography with over-all yield of 17.8%. The molecular weight of native enzyme was 205, 000 by HPLC, and SDS-polyacrylamide gel electrophoresis showed that the enzyme consisted of 4 identical subunits with a molecular weight of 56, 000.

• Microbiology and Biotechnology Letters
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• v.22 no.6
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• pp.627-635
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• 1994

The $\beta$-xylosidase from Penicillium sp. FX-102 was purified by 40~80% ammonium sulfate saturation, CM-Cellulose column chromatography, Sephadex G-200 gel filtration, and isoelec- tric focusing. The optimum pH and temperature for the activity of the $\beta$-xylosidase was pH 4.5 and 50$\circ$C, respectively. The enzyme was stable at the pH range of 4.5~5.5, and at 55$\circ$C for 10 min. The molecular weight of the enzyme was estimated to be about 300,000 daltons by Sephadex G-200 gel filtration and 310,000 daltons of monomer by SDS polyacrylamide gel electrophoresis. Isoelectric point of the enzyme was determined to be pH 4.4. The enzyme activity was strongly inhibited by Hg$^{2+}$, Ag$^{2+}$, n-bromosuccinimide and p-chloromercuribenzoate. Xylobiose (10 mM) was completely decomposed to xylose after 8 hrs enzyme reaction with 2 units of the $\beta$-xylosidase.

• The Korean Journal of Mycology
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• v.10 no.2
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• pp.57-65
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• 1982

Highly phosphorylated nucleotides were investigated to assure whether the eucaryotic Aspergillus niger produce these substances or not during the differentiation. Investigation was extended to see how organic phosphate interacts with inorganic polyphosphate during development, and high molecular weight RNA-polyphosphate complex was detected in 2.6% polyacrylamide gel by electrophoresis. Guanosine tetraphosphate was found in vesicle and phialide forming mycelia and spore forming body by PEI cellulose TLC. It is revealed that guanosine tetraphosphate is a common substance for spore formation in eucaryotic microorganisms as well as in procaryotic. Especially, prior to sporulation, protein bound RNA and protein bound phosphate may occur as a result of reorganization of cellular materials. The evidence was obtained by the fact of differential increase of optical density ratio between the samples from different developmental stages of this fungus. In 2.6% polyacrylamide gel which was run to electrophoresis, high molecular weight RNA (mostly rRNA) was found to couple and to make RNA-polyphosphate complex. The complex was examined with enzymes and radioactive isotope of $^{32}P$. (enzymic test was not reported here.) RNA-polyphosphate complex might be another sort of highly phosphorylated nucleotide or rRNA beside guanosine-tetraphosphate.