• Korean Journal of Pharmacognosy
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• v.40 no.2
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• pp.109-117
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• 2009

We examined the purity of six heparin samples by using heparinase, chondroitinase, $^{1}H-NMR$, and polyacrylamide gel electrophoresis. To obtain high molecular weight contaminants from heparin samples, heparinase I - digested samples were subjected to the exhaustive microcon filtration. The filtration process removed heparin-derived di- and oligosaccharides effectively. By combining chondroitinase ABC treatment and strong anion exchange - high performance liquid chromatography, the result showed all six samples contained chondroitin sulfate as a contaminant ranging from 1.3 to 14.9%. Among them, sample S3 showed the highest content of 14.9%, which was further analyzed by chondroitinase AC treatment to confirm chondroitin sulfate B (dermatan sulfate). $^{1}H-NMR$ chemical shifts of N-acetyl groups clearly suggested the existence of chondroitin sulfate B (sample S3) and oversulfated chondroitin sulfate (samples S2 and S4) as contaminants. In addition, polyacrylamide gel electrophoresis was useful for qualitative detection on the sample's purity. These results suggest that the tools of heparinase I and chondroitinase ABC in combination with NMR spectroscopy would give very useful information for investigation of heparin contaminants such as oversulfated chondroitin sulfate and dermatan sulfate in heparin samples.

• Journal of Soil and Groundwater Environment
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• v.20 no.4
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• pp.31-40
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• 2015

Various types of inorganic and organic colloids are present in natural water including groundwater. Previous studies showed that Fe, Mn and Al are colloid-forming elements and dissolved concentrations can be erroneous for these elements if water samples are not properly filtered. Dissolved concentrations of elements including Ca, Na, Mg, K, Fe, Mn, Si and Al in groundwater from alluvial and bedrock aquifers, and surface water near Nakdong River were determined to evaluate effects of colloids on dissolved concentrations in natural water samples using various pore sizes of filters. Groundwater is mostly anoxic and have elevated concentrations of Fe and Mn, which provides a unique opportunity to observe the effects of colloids on dissolved concentrations of colloid-forming elements. Membrane filters with four kinds of pore sizes of 1000 nm, 450 nm, 100 nm, and 15 nm were used for filtration of water samples. Concentrations of dissolved concentrations in each filtrate did not show significant differences from 1000 nm to 100 nm. However, concentrations of all elements considered were decreased in the filtrates obtained using 15 nm pore size filters by 10 to 15% compared to those using 450 nm except for bedrock groundwater. Al in surface water showed a distinct linear decrease with the decrease of filter pore sizes. These results showed that 100 nm pore size had little effect to remove colloidal particles in alluvial groundwater and surface water in our study. In contrast, significant concentration decreases in 15 nm pore size filtrates indicate that the presence of 15 to 100 nm colloidal particles may affect determination of dissolved concentrations of elements in natural water.

• Korean Journal of Veterinary Research
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• v.11 no.2
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• pp.123-136
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• 1971

(1) The non-specific inhibitors (NSI) in normal chicken sera were active against all the tested group A and group B arboviruses, but the group B arbovirus were more sensitive than group A arboviruses. (2) The titres of the NSI were distributed nearly uniformly among chickens from seven different age groups to group A arboviruses. In contrast, the NSI titres to group A arboviruses were found to increase with age. (3) No significant difference could be demonstrated between acetone-ether extraction and kaolin adsorption for removal of the NSI in normal chicken sera. (4) After heating, the NSI titres in chicken sera were increased for both group A and group B arboviruses. (5) After heating the sera at $80^{\circ}C$ and $100^{\circ}C$, kaolin adsorption was less efficient for removing the NSI than it, was in unheated serum. Acetone-ether extraction of the NSI was unimpaired after heating at $80^{\circ}C$ but was less efficient after heating at $100^{\circ}C$. (6) The NSI activity was found mainly in the first peak (IgM) and diffused to a part of second peak (IgG) by fractionation of chicken serum by gel filtration through Sephadex G200. After zonal centrifugation of chicken serum in a linear ten to 40 percent sucrose gradient all of the NSI activities were found on the top of the centrifugal tubes. These properties of large molecular size and low density indicated that the NSI in chicken serum were probably lipoproteins. (7) The natural agglutinins for goose erythrocytes in chicken sera were partially destroyed by acetone-ether extraction but not by kaolin adsorption, and were efficiently adsorbed with ten percent goose erythrocytes. No difference of the NA titre was demonstrated with diluents of different pH. (8) The NA in chicken serum was found to possess the properties of IgM by gel filtration through Sephadex G200 and zonal centrifugation in linear ten to 40 percent sucrose gradient.

• Journal of the Korean Society of Food Science and Nutrition
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• v.32 no.5
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• pp.745-751
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• 2003

This study was carried out to investigate whether peptide produced from wheat protein by enzyme hydrolysis can be used as a natural antimicrobial agent. Antimicrobial peptide was obtained from wheat protein hydrolyzed by 7 of pretense. The produced antimicrobial peptide was purified through ultrafiltration, membrane filtration and HPLC and molecular weight and amino acid sequence of the purified antimicrobial peptide were determined. Among hydrolysate produced from wheat protein by 7 of protease, antimicrobial activity was observed for the peptide obtained from Asp. saito protease. The Asp. saito protease did produce antimicrobial hydrolysate showing the highest antimicrobial activity at reaction condition of 37$^{\circ}C$ and pH 6.0, but not at reaction condition above 5$0^{\circ}C$. Wheat protein hydrolysate was fractionated by membrane filtration and showed antimicrobial activity between molecular weight 1,000~3,000. The antimicrobial activity fraction obtained by membrane filtration was separated through HPLC and showed antimicrobial activity in the peak of retention time 31.1~31.8 min. We could convince this hydrolysate as heat-stable peptide since antimicrobial activity was maintained after treated with heat for 15 min at 121$^{\circ}C$. Molecular weight of antimicrobial peptide identified by MALDI-mass was 1,633. Amino acid sequence of antimicrobial peptide was cysteine, glycine, prolin, prolin, prolin, valine, valine, alanine, alanine and arginine.

• Korean Journal of Agricultural Science
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• v.29 no.2
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• pp.78-90
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• 2002

This study was carried out to investigate whether peptide produced from wheat protein by enzyme hydrolysis can be used as a natural antimicrobial agent. Antimicrobial peptide was obtained from wheat protein by protease of 7 species. The produced antimicrobial peptide was purified through ultrafiltration, membrane filtration and HPLC, and molecular weight and amino acid sequence of the purified antimicrobial peptide were determined. Among hydrolysate produced from wheat protein by protease of 7 species, antimicrobial activity was observed for the peptide obtained from Asp. saito protease. The Asp. saito protease did production antimicrobial hydrolysate showing the highest antimicrobial activity at reaction condition of $37^{\circ}C$ and pH 6.0, but not at reaction condition above $50^{\circ}C$. Wheat protein hydrolysate was fractionated by membrane filtration and showed antimicrobial activity between molecular weight 1,000 - 3,000. The antimicrobial activity fraction obtained by membrane filtration was separated through HPLC and showed antimicrobial activity in the peak of retention time 31.1 - 31.8 min. Since after wheat protein protease hydrolysate was heated during 15 min at $121^{\circ}C$, antimicrobial activity was maintained, we could be conviction as heat-stable peptide. Molecular weight of antimicrobial peptide identified by MALDI-mass was 1,633. Amino acid sequence of antimicrobial peptide was cysteine, glycine, prolin, prolin, prolin, valine, valine, alanine, alanine and arginine.

• Journal of Microbiology and Biotechnology
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• v.9 no.6
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• pp.861-869
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• 1999

An extracellular protease was purified to homogeneity from the culture supernatant of psychrotrophic bacteria Bacillus sp. JH 108 using procedures including ammonium sulfate fractionation, anion exchange chromatography, gel filtration chromatography, and cation exchange chromatography. The enzyme exhibited a molecular weight of 36 kDa, an optimum pH of 8 to 9, and optimum temperature of $60^{\circ}C$. The enzyme preferentially hydrolyzed leucine at the N-terminus of peptides and thus can be classified as an aminopeptidase. It was strongly inhibited by metal chelating agents such as EDTA and l, l0-phenanthroline. The activity lost by EDTA was restored with $Zn^{2+}{\;}or{\;}Co^{2+}$. These divalent cations also stimulated the native enzyme. This suggests that the enzyme is a metalloprotease acting as a leucine aminopeptidase.

• Journal of Microbiology and Biotechnology
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• v.3 no.3
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• pp.188-193
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• 1993

Superoxide dismutase (SOD) was purified from Pseudomonas polycolor to an electrophoretically homogeneous state and partially characterized. SOD was purified by ammonium sulfate fractionation, column chromatography on DEAE-Sephadex A-50, phenyl-Toyopearl 650 M, and gel filtration on Sephadex G-100. The molecular weight and subunit molecular weight of the purified enzyme were estimated to be 40, 000 and 20, 000, respectively. The purified enzyme remained stable at pH 9.0~11.0, $25^{\circ}C$ for 40 hr, but rapidly became inactive below 9.0. SOD was stable up to $45^{\circ}C$ at pH 9.0 with about 80% relative activity, but rapidly became inactive at temperature above that. The enzyme was insensitive to cyanide and fluoride, and sensitive to hydrogen peroxide and azide. The results suggest that the enzyme be an iron-containing SOD.

• Bulletin of the Korean Mathematical Society
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• v.37 no.1
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• pp.191-207
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• 2000

Let R be a ommutative ring with unity and F a finite free R-module. For a nonnegative integer r, there exists a natural filtration of$S_r(S_2F)$ such that its associated graded module is isomorphic to $\Sigma_{{\lambda}{\epsilon}{\tau}_r}\;L_{\lambda}F$, where ${\Gamma}_{\gamma}$ set of partitions such that $$\mid${\lambda}$\mid$-2r,{{\widetilde}{\lambda}}-{{\widetilde}{\lambda}}_1},...,{{\widetilde}{\lambda}}_k},\;each\;{{\widetilde}{\lambda}}_t}$,is even. We call such filtrations plethysm formulas. We extend the above plethysm formula to the version of chain complexes. By plethysm formula we mean the composition of universally free functors. $Let{\emptyset}:G->F$ be a morphism of finite free R-modules. We construct the natural decomposition of $S_{r}(S_2{\emptyset})$,up to filtrations, whose associated graded complex is isomorphic to ${\Sigma}_{{\lambda}{\varepsilon}{\tau}}_r}\;L_{\lambda}{\emptyset}$.

• Membrane Journal
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• v.29 no.3
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• pp.147-154
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• 2019

The permeate flux increments of a natural convection instability flow (NCIF) caused by the change of inclined angles ($0{\sim}180^{\circ}$) to gravity of the commercial membrane module were tested in the dead-end membrane filtration of BSA protein solution. The NCIF are more generated as the inclined angle increased from $0^{\circ}$ to $180^{\circ}$, and the occurred NCIF enhances permeate flux. However, the commercial module can only generate NCIF by completely removing the air gap in module. Since the custom design module designed in this study is permeated in a crossward direction ($90^{\circ}$), NCIF is always generated even if there is the air gap in module. The results of membrane filtration of BSA and dextran solutions using a custom design module showed that the flux in the crossward direction is increased to about 3.8 times for BSA solution and 1.8 times for dextran solution after two hours of operation due to the occurrence of NCIF. Also, NCIF generation is continued during 20 hours filtration of BSA solution, increasing the permeate flux to about 7.5 times. Since the custom design module with a permeation in the crossward direction and NCIF is always generated within the module, so it is possible to expect an increase in permeate flux due to the suppression of fouling formation, and thus to be utilized as a superb dead-end membrane module.

• Journal of Microbiology and Biotechnology
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• v.7 no.2
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• pp.121-126
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• 1997

A bacterial strain LC-413, producing an extracellular inulin fructotransferase (depolymerizing) which converts inulin into di-D-fructofuranose dianhydride (DFAIII), was isolated from soil. Inulin fructotransferase from the isolate identified as a strain Flabobacterium sp. was purified from the culture broth by ammonium sulfate precipitation, followed by column chromatograpies on DEAE-Toyopearl 650 M and phenyl-Toyopearl 650 M. The purified enzyme gave a single band on an electrophoretic disc-gel. The molecular weight of the enzyme was estimated to be 44, 000 Da by SDS-polyacrylamide gel electrophoresis, and 45, 000 Da by gel filtration, suggesting the monomeric state of the enzyme. The isoelectric point of the enzyme was about pH 4.5. The optimal pH and temperature for the enzyme reaction were 6.0 and $50^{\circ}C$, respectively. The purified enzyme digested inulin into di-D-fructofuranose-l, 2': 2, 3'-dianhydride, confirming the enzyme was an inulin fructotransferase (inulinase II).