• Korean Journal of Microbiology
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• v.32 no.4
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• pp.297-300
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• 1994

About thirty bacterial strains of actinomycete isolated from the soil were examined for the presence of restriction endonuclease activity. Streptomyces diastatochromogenes, which was identified previously, was found to contain restriction endonuclease activity. The purification of this enzyme, SdiI, was carried out via streptomycin sulfate precipitation and ammonium sulfate fractionation followed by hydroxylapatite column chromatography. Sephacryl S-200 HR column chromatography and second hydroxylapatite column chromatography. SDS-polyacrylamide gel electrophoresis of the active protein (purified from various column chromatography) resulted in 35,000 Da protein.

• Proceedings of the Plant Resources Society of Korea Conference
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• 2001.11b
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• pp.70-70
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• 2001

• BMB Reports
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• v.28 no.3
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• pp.238-242
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• 1995

The tadpole H-ferritin produced in E. coli was purified and its molecular properties were investigated to obtain information about the contribution of the H-subunit in the reaction of iron core formation. All the expressed subunits were assembled into complete holoprotein in vitro, presumably 24-mer, and the protein was heat-stable. Electron microscopy revealed that the recombinant ferritin forms spherically and contains iron core. No difference was observed in the absorption spectrum of the expressed protein compared to that of the natural ferritin. The Ouchterlony double diffusion of the expressed protein showed that the H-chain ferritin shares an antigenic determinant with natural tadpole ferritin. Rabbit anti-horse spleen ferritin discriminated the H-ferritin from natural ferritin. The rate of ferritin formation by the recombinant H-chain apoferritin was determined to be higher than that shown by natural tadpole ferritin, which consists of H, M and L-subunits. This phenomenon may be caused by the absence of M and L-subunits in the recombinant H-chain apoferritin.

• 한국신재생에너지학회:학술대회논문집
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• 2011.05a
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• pp.172-172
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• 2011

Anaerobic digestion(AD) has successfully been used for many applications that have conclusively demonstrated its ability to recycle biogenic wastes. AD has been successfully applied in industrial waste water treatment, stabilsation of sewage sludge, landfill management and recycling of biowaste and agricultural wastes as manure, energy crops. During AD, i.e. organic materials are decomposed by anaerobic forming bacteria and fina1ly converted to excellent fertilizer and biogas which is primarily composed of methane(CH4) and carbon dioxide(CO2) with smaller amounts of hydrogen sulfide(H2S) and ammonia(NH3), trace gases such as hydrogen(H2), nitrogen(N2), carbon monoxide(CO), oxygen(O2) and contain dust particles and siloxanes. The production and utilisation of biogas has several environmental advantages such as i)a renewable energy source, ii)reduction the release of methane to the atomsphere, iii)use as a substitute for fossil fuels. In utilisation of biogas, most of biogas produced from small scale plant e.g. farm-scale AD plant are used to provide as energy source for cooking and lighting, in most of the industrialised countries for energy recovery, environmental and safety reasons are used in combined heat and power(CHP) engines or as a supplement to natural. In particular, biogas to use as vehicle fuel or for grid injection there different biogas treatment steps are necessary, it is important to have a high energy content in biogas with biogas purification and upgrading. The energy content of biogas is in direct proportion to the methane content and by removing trace gases and carbon dioxide in the purification and upgrading process the energy content of biogas in increased. The process of purification and upgrading biogas generates new possibilities for its use since it can then replace natural gas, which is used extensively in many countries, However, those technologies add to the costs of biogas production. It is important to have an optimized purification and upgrading process in terms of low energy consumption and high efficiency giving high methane content in the upgraded gas. A number of technologies for purification and upgrading of biogas have been developed to use as a vehicle fuel or grid injection during the passed twenty years, and several technologies exist today and they are continually being improved. The biomethane which is produced from the purification and the upgrading process of biogas has gained increased attention due to rising oil and natural gas prices and increasing targets for renewable fuel quotes in many countries. New plants are continually being built and the number of biomethane plants was around 100 in 2009.

• Proceedings of the Zoological Society Korea Conference
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• 1999.10b
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• pp.241.2-241
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• 1999

No Abstract, See Full Text

• Journal of the Korean Institute of Landscape Architecture
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• v.34 no.3 s.116
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• pp.1-11
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• 2006

This study analyzed characteristics of natural and human environments in Chuncheon's Gongji stream, and suggested nature-friendly planning strategies for self-purification of water quality, biodiversity improvement and conservative waterfront recreation. The environmental analysis included streambed structures, floodplain soils, water quality, vegetation, wildlife, and human facilities. Natural colonization of vegetation for the middle section of the study stream was obstructed by a straightened concrete revetment of baseflow channel, and vehicle movement and concrete parking lots across the floodplain. These human disturbances also deteriorated the naturalness of the stream landscape and limited habitation of bird species. However, natural sedimented wetlands in half of the channel width for the lower section of the stream contributed to a desirable vegetational landscape and greater bird occurrence. Based on BOD measurements, water quality of the stream fell under class $II{\sim}III$ of the stream water-quality standard, but it was worse around sewage outlets due to incomplete sewage collection especially during the dry season. Dominant fish species included typical inhabitants of good water-quality streams that are tolerant of adverse habitat changes. Nature-friendly planning strategies were established based on analysis of the environmental characteristics. They focused on not merely spatial zoning and layout divided into four zones - preservation, partial preservation, conservation and use -, but close-to-nature channel revetment techniques, natural water-purification facilities, biotope diversification, and water-friendly recreation and circulation. Strategies pursued both renewal of stream naturalness and hydraulic stability of streamflow by minimizing transformation of natural channel micro-topography and biotope, and by reflecting natural traces of streambed structures such as revetment scour and sedimentation.

• Journal of Microbiology
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• v.37 no.1
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• pp.21-26
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• 1999

Two novel calcium-binding proteins, named CAB-I and CAB-II, have been isolated from Streptomyces coelicolor. Purification of the calcium-binding proteins involved heat treatment, fractionation with ammonium sulfate, acid treatment, anion exchange and hydrophobic interaction column chromatography, FPLC gel filtration, and preparative isoelectric focusing. A chelex competitive assay and 45Ca autoradiography verified the calcium-binding ability of the proteins. The major band CAB-II has an apparent molecular weight of 26,000 determined by SDS-polyacrylamide gel electrophoresis and 340,000 determined by gel filtration. The isoelectric point of this molecule showed the acidic nature of the molecule. N-terminal amino acid sequence analysis shows homology to rat Ca2+/calmodulin-dependent protein kinase-II (CAB-II) and yeast phosphoprotein phosphatase (CAB-I).

• BMB Reports
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• v.38 no.2
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• pp.232-237
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• 2005

A glutathione S-transferase (GST) from Lactuca sativa was purified to electrophoretic homogeneity approximately 403-fold with a 9.6% activity yield by DEAE-Sephacel and glutathione (GSH)-Sepharose column chromatography. The molecular weight of the enzyme was determined to be approximately 23,000 by SDS-polyacrylamide gel electrophoresis and 48,000 by gel chromatography, indicating a homodimeric structure. The activity of the enzyme was significantly inhibited by S-hexylGSH and S-(2,4-dinitrophenyl) glutathione. The enzyme displayed activity towards 1-chloro-2,4-dinitrobenzene, a general GST substrate and high activities towards ethacrynic acid. It also exhibited glutathione peroxidase activity toward cumene hydroperoxide.

• BMB Reports
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• v.30 no.6
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• pp.410-414
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• 1997

We purified a protein carboxyl O-methyltransferase (protein methylase II) from porcine spleen to homogeneity. The molecular weight of the porcine spleen protein methylase II (ps-PM II) was estimated to be 27,500 daltons on SDS-PAGE. Amino acid sequence of N-terminal 28 residues for ps-PM II was identified. Amino-terminal three amino acid residues of ps-PM II were deleted when compared to those of other protein carboxyl methytransferase. S-Adenosyl-L-homocysteine competitively inhibits ps-PM II with a K, value of $1.63{\times}10^{-7}M$. Myelin basic protein exhibited the highest methyl-accepting capacity among the proteins tested.

• BMB Reports
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• v.31 no.2
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• pp.135-138
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• 1998

A previous study on a yeast protein tyrosine phosphatase, YPTP1, using synthetic phosphotyrosine-containing peptides with various sequences as substrates revealed that DADEpYDA exhibits high affinity ($K_m=4{\mu}M$) toward the enzyme. A modified version of this peptide, GDADEpmFDA, immobilized on a resin, was used in this study as an affinity ligand for the purification of YPTP1. Phosphonomethyl-phenylalanine (pmF) was used as a nonhydrolyzable analog of the phosphotyrosine (pY) residue, with properties similar to pY. A protected form of pmF, $Fmoc-pmF(^{t}Bu)_{2}-OH$, was chemically synthesized and introduced during solid-phase peptide sythesis. YPTP1 was onrexpressed in an E. coli strain carrying a plasmid pT7-7-ptpl. Affinity chromatography of the crude lysate afforded PTPI (39 kDa) of about 50% purity.