• Journal of the Korea Society for Simulation
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• v.20 no.2
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• pp.77-85
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• 2011

It is believed that the anomalies or diseases of human organs are identified by the analysis of the patterns. This paper proposes a new classification technique for the identification of cancer disease using the proteome patterns obtained from two-dimensional polyacrylamide gel electrophoresis(2-D PAGE). In the new classification method, three different classification methods such as support vector machine(SVM), multi-layer perceptron(MLP) and k-nearest neighbor(k-NN) are extended by multi-boosting method in an array of subclassifiers and the results of each subclassifier are merged by ensemble method. Genetic algorithm was applied to obtain optimal feature set in each subclassifier. We applied our method to empirical data set from cancer research and the method showed the better accuracy and more stable performance than single classifier.

• KSBB Journal
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• v.5 no.2
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• pp.141-149
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• 1990

$\beta$-glucosidase derived from Aspergillus niger was immobilized by (1) covalent linkage on chitin and chitosan with glutaraldehyde, (2) adsorption on DEAE-cellulose and Amberite IRA93 after succinylation, and (3) entrapment on alginate and polyacrylamide gels with various cross linking agents. The retention yield of $\beta$-glucosidase immobilized on chitosan was 31.5% and operational stability was 69% after continuous operation at column reactor(5$0^{\circ}C$ at pH 4.8) for 15 days. The retention yield and operational stability were 24.7% and 60% respectively, in adsorption on Amberite IRA 93. On the other hand, the entrapment method by alginate and polyacrylamide gel was identified to be not appropriate due to the continuous elution of inlmobilized $\beta$-glucosidase. Optimum conditions for the immobilization on chitosan were also studied with optimum pH of 4.8 and glutaraldehyde concentration of 0.4%(w/v). The properties and stability of immobilized $\beta$-glucosidase are also investigted. The conversion yield of cellobiose to glucose was also analyzed using the column type enzyme reactor to evaluate the effectiveness of immobilized enzyme.

• The Korean Journal of Zoology
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• v.33 no.2
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• pp.191-199
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• 1990

Sarcoplasmic reticulum subfractions were isolated from rabbit sarcoplasmic reticulum vesicles using ultracentrifugation in a continuous sucrose gradient (12.5% 50%) after French pressure treatment. And proteins in sarcoplasmic reticulum were detected by SDS-polyacrylamide gel electrophoresis and glycoproteins were identified through the reaction with 1251-concanavalin A.The electrophoresis showed that sarcoplasmic reticulum contained predominantly $Ca^2$+-AThase and calsequestrin along with high affinity calcium binding protein, intrinsic glycoprotein 160 Kd, 94 Kd, 80 Kd, 38 Kd, 34 Kd and 24 Kd proteins. Among these, the protein of about 80 Kd which has been known as one of heat shock proteins was especially enriched in the terminal cistemae of sarcoplasmic reticulum. Meanwhile, autoradiogram of 125 I-concanavalin A bound to the stained gels showed the distribution of glycoproteins which included 160 Kd glycoprotein, 94 Kd glycoprotein, calsequestrin and intrinsic glycoprotein Among these, the protein of about 160 Kd was especially enriched in longitudial sarcoplasmic reticulum and T-tubule, and the protein of about 94 Kd which has been known as one of glucose-regulated proteins was also enriched in T-tubule and sharply reduced in terminal cistemae.

• Korean Journal of Food Science and Technology
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• v.19 no.5
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• pp.397-402
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• 1987

Two lipoxygenases (F-I and F-II) were purified from potato tubers by ammonium sulfate fractionation and ion-exchange column chromatographies. The purified isoenzymes were apparently homogeneous on polyacrylamide gel electrophoresis. Both enzymes showed a similar optimum pH of 5.5-6.0. From thermal inactivation experiments with the purified enzymes in the range of 50 to $65^{\circ}C$, D-values of 13.3 min and 4.3 min at $65^{\circ}C$, and z-values of $11.8^{\circ}C\;and\;10.3^{\circ}C$ were obtained respectively for F-I and F-II. By applying absolute reaction rate equation, thermodynamic parameters wire also determined for the activation part of the inactivation process.

• Korean Journal of Food Science and Technology
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• v.21 no.5
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• pp.726-734
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• 1989

To analyze the components of dense coat fractions associated with fat globule membrane, The membrane was treated with various concentrations of Triton X-100, a non-ionic detergent, and the composition of lipids associated to the detergent insoluble material was analyzed. The amount of protein, phospholipid, cholesterol and ganglioside in milk fat globule membrane was reduced consistently with increasing concentrations of Triton X-100. Butyrophilin (band 12), xanthine oxidase (band 3) and band 16 as constituents of insoluble coat materials was revealed after electrophorisis on SDS-polyacrylamide gels. Phosphatidyl ethanolamine, phosphatidyl choline, phosphatidyl serine, phosphatidyl inositol and sphingomyelin were identified as the major phospholipids of the coat materials without selective concentration relative to the original membranes. Percentages of total phospholipid were not changed by any of the treatments. Fatty acids of total lipid were myristate, palmitate, stearate (major saturated acids), oleate and linoleate (major unsaturated acids). Cholesterol contents on a protein basis were slightly reduced with increasing concentrations of Triton X-100. Cholesterol adhered to protein more tightly than other constituents The contents of gangliosides was proportionally refuted with increasing concentration of Triton X-100.

• Korean Journal of Microbiology
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• v.25 no.3
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• pp.180-183
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• 1987

Stu I, type II restriction endonuclease, has been purified to homogeneity from Streptomyces tubercidicus (ATCC 25502), and its catalytic properties have been studied. For the purification of Stu I endonuclease free of nonspecific nucleases, DEAE-Sephadex (A-50), QAE-Sephadex (A-50) and Heparin-agarose column chromatography have been performed after ammonium sulfate fractionation of the crude extract. The enzyme was further purified by gel filtration using Sephadex G-100 column to obtain homogeneous form of protein. The single polypeptide species of Stu I endonuclease has a subunit molecular weight of 34,000 $\pm$ 1,000 daltons as judged by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Stu I endonuclease requires $Mg^{2+}$ ion for its activity and is maximally active at neutral pH (7.0-8.0) in the absence of NaCl.

• Korean Journal of Microbiology
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• v.25 no.1
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• pp.23-27
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• 1987

Low molecular weight plant ribonucleic acids including viroid-RNA molecules which are soluble in 2M lithium chloride were electrophoresed in the 0M to 8M urea-gradient polyacrylamide gel. Although the linear viroid-RNA molecules migrated at a similarrate across the urea-gradient gel under the denaturing temperature, the circular viroid-RNA molecules moved more rapidly at low urea-gradient region than at high urea-gradient region. Consequently, the migration of the circular viroid-RNA molecules showed a sudden shift across the band of linear forms in the midrange of the urea-gradient gels. Electrophoretic mobilities of the circular viroid-RNA molecules seemed to depend mainly on the concentration of urea in the denaturing urea-gradient gels.

• Korean Journal of Microbiology
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• v.27 no.4
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• pp.348-356
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• 1989

An extracellular peroxidase found in culture broth of Pleurotus ostreatus was induced by syringic acid. This enzyme was fractionated by DEAE Sephadex A-50 ion exchange chromatography and gel filtration chromatogrphy on Sephadex G-150. The enzyme is a glycoprotein containing 35.7% carbohydrate. The results of SDS-linear polyacrylamide gradient gel electrophoresis and gel filtration indicate that the enzyme is a dimer consisted of identical subunits (Mr=72,400). The absorption spectrum of the enzyme indicates the presence of one mole of iron protoporphyrin IX per one mole of subunit. Isoelectric point of the enzyme is 4.26 and $K_m$ values for $H_2O_2$ is $7.2{\mu}M$. The enzyme showed its optimal activity at pH 3.5-4.0 and at $40^{\circ}C$. The Km values of this enzyme for ferulic acid and sinapic acid are 2.4 and 12.3 times higher than those of horseradish peroxidase, respectively.

• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.2
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• pp.187-194
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• 1992

Rhizopus oryzae CJ-2114 was selected for its strong polygalacturonase activity among various strains of mold found in soil. It was found that the production of polygalacturonase reached to maximum when the wheat bran medium containing 1% albumin, 1% sorbitol and 0.2% (NH$_4$)$_2$C$_2$O$_4$was cultured for 96 hrs at 3$0^{\circ}C$. Polygalacturonase was purified 11.13 fold from Rhizopus oryzae CJ-2114. The purification procedures include ammonium sulfate treatment, gel filtration on Sephadex G-75, G-150 and DEAE-cellulose ion exchange chromatography. Yield of the enzyme purification was 40.3% .Purified enzyme was confirmed as a single band by the polyacrylamide gel electrophoresis. When the purified enzyme was applied to SDS-poly-acrylamide gel electrophoresis, the molecular weight was estimated to be 47,000. The amino acid composition indicated relatively high contents of glutamic acid and glyrine.

• Microbiology and Biotechnology Letters
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• v.30 no.1
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• pp.33-38
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• 2002

Purification and characterization of enzyme property of a cell-wall lytic enzyme against Lactobacillus plantarum were carried out. Final specific activity of purified enzyme was 5.8 units/mg and purity of the enzyme was increased 8.3 fold compared with the enzyme activity in culture broth. The molecular weight of purified enzyme was estimated to be 60,000 kDa by gel filtration and SDS-polyacrylamide gel electrophoresis. Optimal pH and temperature for the activity of this enzyme were 3.0 and 4$0^{\circ}C$, respectively. The cell-wall lytic enzyme activity was maintained at 3$0^{\circ}C$ when treating the enzyme for 30 mins, whereas the activity was decreased to 80% of the maximum level at 4$0^{\circ}C$ The enzyme activity exhibited good stability at the range of pH 4~7.