• 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.

• Korean Journal Plant Pathology
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• v.11 no.4
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• pp.318-323
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• 1995

The effect of AF-toxin I produced by the strawberry pathotype of Alternaria alternata on the protein synthesis of susceptible strawberry protoplasts was examined by using the radiolabeled amino acids. The incorporation of the radiolabeled amino acids into newly synthesized proteins in the strawberry protoplasts was stimulated by the toxin treatment at relatively low concentrations (2.2$\times$10-11 to 2.2$\times$10-9 M), but not at higher concentrations (2.2$\times$10-8 to 2.2$\times$10-6 M). An one-dimensional SDS-polyacrylamide gel electrophoresis revealed no detectable differences in the proteins synthesized in both the toxintreated and untreated protoplasts. The susceptible strawberry protoplasts were treated with AF-toxin I and stained with Fluostain I to detect the extracellular polysaccharides. The toxin treatment induced the accumulation of extracellular polysccharides in a dose-dependent manner. These results indicate a transient activation of cellular metabolism in the susceptible cells by the toxin exposure.

• KSTLE International Journal
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• v.8 no.1
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• pp.16-20
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• 2007

This study introduces a new approach to a falling ball viscometer by using a high speed motion camera to measure the viscosity of both Newtonian and non-Newtonian fluids from the velocity-time data. This method involves capturing continuous photographs of the entire falling motion of the ball as the ball accelerates from the rest to the terminal velocity state. The velocity of a falling ball was determined from the distance traversed by the ball by examining video tape frame by frame using the marked graduations on the surface of the cylinder. Each frame was pre-set at 0.01. Glycerin 74% was used for Newtonian solution, while aqueous solutions of Polyacrylamide and Carboxymethyl Cellulose were for non-Newtonian solutions. The experimental viscosity data were in good agreements with the results obtained from a rotating Brookfield viscometer.

• Journal of the Korean Society of Tobacco Science
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• v.12 no.1
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• pp.9-18
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• 1990

To study the determinants which are involved in the loss of pathogenicity in wilt-inducing Pseudomoms solamcewum, several physlologica I functions were compared in a virulent P. solanacearum strain and an avirulent, spontaneously derived mutant strain. The polyacrylamide gel electrophoresis showed the distinction between two strains in the patterns and the relative intensity of proteins produced intracellularly or extracellularly. Enzyme assays showed that the level of polygalacturonase activity in the culture filtrate of the avirulent mutant was markedly reduced, while carboxymethylcellulase(rondoglucanase) activity in both strains were nearly negligible. These results suggest that the loss of pathogenicity in mutant strain is attributed in part to the reduced production of polygalacturonase. In audit ion, comparative analyses by agarose gel electrophoresis of DNA molecules isolated from both strains show that the pathogenicity genes of p. solanaceerum are not located on plasmid but are on chromosome.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.34 no.4
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• pp.7-15
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• 2002

It is of critical importance to understand the characteristics of papermaking additives and their reaction mechanisms to fully utilize the benefits they provide. Among the papermaking additives, retention aids play critical roles in improving productivity, product quality and process economy. Diverse research efforts to understand the reaction mechanisms between cationic polymers and anionic microparticles have been made since microparticle retention systems were introduced into the market. And it is most commonly accepted that flocs formed by the addition of cationic polymers are dispersed by shear force and the broken flocs are reflocculated instantly with the addition of microparticles. There are still many unanswered questions, however, on the reaction phenomena between cationic polymers and anionic microparticles. In this study, several cationic polymers including waxy maize starch, com starch and guar gum were used to investigate their retention efficiency when they were used along with anionic colloidal silica.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.33 no.2
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• pp.1-7
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• 2001

Use of high yield pulp and recycled fiber as raw materials and water system closure result in higher fines content and buildup of organic and inorganic contaminants in white water. These are detrimental for the effectiveness of chemical additives including retention aids. Thus it is imperative to employ a retention systems that maintains its efficiency in closed papermaking system for reducing fresh water consumption. The performance of four different microparticle retention systems including cationic polyacrylamide (C-PAM)/bentonite, highly charged cationic starch (HCS)/silica, C-PAM/micropolymer, cationic guar gum (CGG)/silica was evaluated and compared at three different levels of papermaking system closure. Buildup of detrimental substances in a closed white water system increased cationic demand and finally reduced the performance of retention systems. Cationic starch and guar gums maintained their effectiveness in retention in closed white water systems contaminated with anionic trashes because of their structural rigidity and hydrogen bonding ability. Particularly, cationic guar gums, due its stiffness of molecular structure, appeared perform better than catinonic starch.

• Journal of Microbiology
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• v.42 no.1
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• pp.20-24
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• 2004

Cloned myo-inositol-1-phosphate synthase (INOS) of Drosophila melanogaster was expressed in Escherichia coli, and purified using a His-affinity column. The purified INOS required NAD$\^$+/ for the conversion of glucose-6-phosphate to inositol-1-phosphate. The optimum pH for myo-inositol-1-phosphate synthase is 7.5, and the maximum activity was measured at 40$^{\circ}C$. The molecular weight of the native enzyme, as determined by gel filtration, was approximately M$\_$r/ 271,000${\pm}$15,000. A single subunit of approximately M$\_$r/ 62,000${\pm}$5,000 was detected upon SDS-polyacrylamide gel electrophoresis. The Michaelis ($K_{m}$) and dissociation constants for glucose-6-phosphate were 3.5 and 3.7 mM, whereas for the cofactor NAD$\^$+/ these were 0.42 and 0.4 mM, respectively.

• Korean Journal of Microbiology
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• v.24 no.2
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• pp.119-126
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• 1986

A periplasmic endoprotease, named protease Pi, was purified to homogeneity from Escherkchia coli by conventional procedure with insulin as substrate. This enzyme degrades insulin and glucagon to trichloroacetic acid-soluble meterials, but shows little or no hydrolysis of bovine serum albumin, casein or globin. Its molecular weight was 110, 000 when determined by gel filtration on Sephacryl S-300 and was 105, 000 when estimated by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Thus, it appears to be single polypeptide. This snzyme is metalloprotease, since it is completely inhibited by o-phenanthroline and can be activated by addition of divalent metal cations, such as $Mg^{2+}\;and\;Co^{2+}$. It is destinct from protease Ci, a cytoplasmic insulin degrading enzyme, since protease Pi is localized to the periplasm. Since protease Pi selectively degrades GTP cyclohydrolase I, it appears to play a role in the regulation of pteridine biosynthesis.

• Korean Journal of Microbiology
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• v.28 no.1
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• pp.65-70
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• 1990

The objective of the current study is to elucidate the biological roles of proteinase inhibitor in microorganisms. As the first step, a strain of Streptomyces fradiae was selected as a producer of extracellular proteinase inhibitor. The proteinase inhibitor was purified from culture broth through ultrafiltration, gel-filtration and ion-exchange chromatography. Molecular weight of the proteinase inhibitor was estimated to be 16, 800 by SDS polyacrylamide gel electrophoresis. It was found that the proteinase inhibitor inhibited only alkaline serine proteinases such as subtilisin, $\alpha$-chymotrypsin and Promase E but not trypsin and other proteinases. The mode of inhibition against Pronase E with succinyl-phenylalanine-p-nitroanilide as a substrate was competitive.

• BMB Reports
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• v.28 no.2
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• pp.143-148
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• 1995

In E. coli, chromosomal DNA associated with proteins is condensed into an organized structure known as nucleoid. Using a nitrocellulose filter binding assay to identify proteins forming nucleoid, a 21 kDa protein was purified from E. coli. The molecular weight of the purified protein was 21 kDa on SDS-polyactylamide gel electrophoresis and 24 kDa on gel permeation chromatography. A molecular weight of 21 kDa on SDS-polyacrylamide gel electrophoresis is unique among known proteins which are believed to be involved in the formation of nucleoid in E. coli. The 21 kDa protein nonspecifically binds to both double-stranded and single-stranded DNA. Sedimentation in a sucrose gradient revealed that the protein induced significant condensation of both supercoiled plasmid DNA and linear bacteriophage $\lambda$ DNA On the basis of quantitative Western-blot analysis, approximately 40,000 molecules of the protein were estimated to exist in an E. coli. The biochemical properties and cellular abundance of the 21 kDa protein suggest that this protein participates in the formation of nucleoid in E. coli.