• The Korean Journal of Mycology
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• v.20 no.1
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• pp.72-76
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• 1992

The extraction and separation methods of protein-bound polysaccharides from the mycelium and culture broth of Coriolus versicolor (Fr) Quel were investigated. The use of 2% solution of surface active agent Triton X-100, was effective for extraction of the protein-bound polysaccharides from the mycelium. For the separation and partial purification of the protein-bound polysaccharides, the column chromatography using DEAE-Cellulose and DEAE-Sephadex proved to be effective.

• Applied Biological Chemistry
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• v.20 no.1
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• pp.136-141
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• 1977

DEAE-Cellulose, Sephadex column chromatography and polyacrylamide gel electrophoresis were used to purify acid phosphatase, aryl sulfatases, ${\beta}-glucuronidase$ and cathepsin D in n-butyl alcohol extracts of porcine leukocyte Iysosomes. The degree of purification was quite high for all enzymes studied and some could be identified by histochemical reactions.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.6
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• pp.777-784
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• 1993

The bleaching effect of potato lipoxygenase Isoenzymes on ${\beta}-carotene$ was studied. Two lipoxygenase Isoenzymes(LOX-1, LOX-2) from potato tuber were purified by CM-cellulose, DEAE-cellulose ion exchange chromatography. LOX-1 and LOX-2 seemed to have bleaching effect on ${\beta}-carotene$ in the presence of linoleic acid, which the decrease in the formation of conjugated dienes. LOX-2 was founded to have a greater pigment bleaching activity than that of LOX-1.

• ALGAE
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• v.22 no.2
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• pp.125-129
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• 2007

Conventional methods for the isolation and purification of mRNA from Zygnema were unsuccessful because of its high amount of pigments and RNA interactive molecules. In particular, pigments were difficult to remove using conventional protocols because they interacted with RNA during pulverization of the materials. This resulted in total degeneration of RNA in two to three hours. To alleviate this problem, we developed an isolation method that utilized DEAE-cellulose resin. The pigments bound to DEAE anion exchange resin and separated from the RNA. Purified total RNA showed an yield of 50 μg per 100 mg of tissue with this method. The amplified 2nd strand cDNA was distributed 300 bp and over.

• Korean Journal Plant Pathology
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• v.14 no.6
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• pp.559-562
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• 1998

Odontoglossum ringspot virus (ORSV) was finally purified from ORSV-infected orchid plants by diethylaminoethyl (DEAE) cellulose anion exchange column chromatography. The virus was reliably eluted by potassium chloride at the concentration from 0.1 M to 0.13 M. Partial purification was done by solubilization with Triton X-100 (allkylphenoxypolyethoxy ethanol) and precipitation with polyethylene glycol (PEG; MW 8,000). The finally purified ORSV represented one distinct homogeneous band and the molecular weight of its capsid protein was about 17,500 Dalton in electrophoretic analysis. Electron microscopy showed not only intact particles ranged from 280 nm to 340 nm in length, but also segmented particles that final 140 nm to 220 nm and even disks. Enzyme-linked immunosorbent assay (ELISA) showed that final yield was 12 mg/100 g of the infected leaves. Bioassay demonstrated that the purified ORSV had the normal infectivity to orchid plants and Nicotiana glutionsa. Based on these data, anion exchange column chromatography could be efficiently applied to the purification of ORSV and other viruses similar to ORSV.

• Applied Biological Chemistry
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• v.12
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• pp.33-41
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• 1969

1. Crude cellulase extracted from wheat bran media of Chaetomium globosum with pH 7.0 McIlvaine buffer was fractionated by precipitation with ammonium sulfate and by treatment with the cellulose powder, DEAE-Sephadex A-25 and Amberite XE-65 (IRC-50) column chromatography. 2. Consquently two cellulases C-1 and C-2 were obtained by cellulose column chromatography. Cellulose C-1 was a powerful CMC-saccharifying and CMC-liquefying activity but cellulose C-2 was stronger CMC-liquefying activity compared to CMC-saccharifying activity and cellulase C-2 had smaller protein than that of cellulose C-1. And cellulose C-2 was fractionated by DEAE-Sephadex A-25 column chromatography into cellulase C-1-1 and cellulose C-1-2. 3. It can be obtained, therefore, that cellulose produced Chaelomium globosum consisted, at least, of three cellulases C-2, C-1-1 and C-1-2. 4. Cellulose C-1-1 was homogenous in the ultraviolet and the ultracentrifuge pattern. And cellulose C-1-1 had enzyme for CMC-saccharifying activity. 5. The optimum pH for the enzyme activity of cellulose C-1-1 was 4.0 in any methods of meas urement reducing sugar and viscosity. The optimum temperature was $40^{\circ}C$ in any methods. 6. The pH stability of cellulase C-1-1 was within pH 5.0 to pH 6.0 at $40^{\circ}C$ and fairly stable in acidic solution. 7. The heat stability was below $50^{\circ}C$ at pH 4.0 and complete heat inactivation of this cellulase occurred at $70^{\circ}C$.

• Korean Journal of Microbiology
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• v.16 no.1
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• pp.30-40
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• 1978

Detergent soluble fractions were obtained from T. ferrooxidans ATCC 13598 and the T. thiooxidans ATCC 8085 which were treated with 3% of Tween 20. The detergent soluble antigen(crude antigen) fractions of the T.ferrooxidans and the T.thiooxidans were subjected to hydroxyapatite. In the case of T.thiooxidans, further purification was carried out on the DEAE-cellulose column chromatography. The antigen fractions, such as the hydroxyapatite peak-1(Tf, HA-1) and peak-2 from T.ferrooxidans(Tf. HA-2) and hydroxyapatite peak-1(Tt, HA-1), DEAE-cellulose peak-1(Tt, DP-1) and peak-2(Tt, DP-2) from T. thiooxidans wre compared each other with the homologous and the heterologous and the heterologous antisera against to the Thiobacillus species. The hydroxyapatite peak-2 fraction from the T.ferrooxidans(Tf, HA-2) and DEAE-cellulose peak-2 fraction from the T.thiooxidans(Tt, DP-2) were represented the type-specific immuno-reactivities between the T.ferrooxidans and the T.thiooxidans on the several sets of double gel diffusioin analysis. The type-specific antigen fractions from both of the baceteria were mainly composed of protein with entierly different electrophoretic mobility on the SDS-polyacrylamide gel electrophoresis. However, the PAS positive banding patterns on the electrophorogram showed wide range of common antigenic properties in the T. ferrooxidans and the T.thiooxidans, respectively.

• Journal of the Korean Society of Food Science and Nutrition
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• v.16 no.2
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• pp.128-135
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• 1987

Extracellular ${\alpha}-amylase$, ${\beta}-amylase$ and glucoamylase produced by a thermophilic and cellulolytic bacterium, Herpetosiphon geysericola CUM 317, were partially purified by salting out with ammonium sulfate and by chromatography on a DEAE-cellulose column and on a CM-cellulose column. The Km values of ${\alpha}-amylase$, ${\beta}-amylase$ and glucoamylase for potato starch were $2.31mg/m{\ell}$, $7.69mg/m{\ell}$, and $8.33mg/m{\ell}$. The molecular weights of ${\alpha}-amylase$, ${\beta}-amylase$ and glucoamylase were calculated to be about 84000 dalton, 76000 dalton and 80000 dalton, respectively.

• Microbiology and Biotechnology Letters
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• v.15 no.5
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• pp.306-311
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• 1987

After series of purification by means of ammonium sulfate fractionation, the 1st and 2nd DEAE-Cellulose, DEAE-Sephadex A-50, and Sephacryl S-200 superfine gel filtration, the activity of extracellular adenine deaminase from Streptomyces sp. J-350P increased 1764 fold and the yield was 0.3% of original activity. The enzyme was stable at the pH range 6.5 to 8.5 and at up to 5$0^{\circ}C$. The optimum pH and temperature of the enzyme were around 6.5 and 35$^{\circ}C$. The molecular weight ol the enzyme was estimated as 36, 000 by calibrated Sephacryl S-200 superfine column chromatography.

• Microbiology and Biotechnology Letters
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• v.8 no.2
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• pp.125-133
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• 1980

A microorganism which produced D-glucose isomerase was identified to be similar to Streptomyces antibioticus on the morphological, cultural and physiological characteristics except the spore chain and the utilization of sucrose. D-xylose grown cells of Streptomyces sp. strain K-17 were disrupted by grinding with sea sand. D-glucose isomerase was partially purified with the fractionation by ammonium sulfate, Mn-treatment, DEAE-cellulose column chromatography, DEAE-sephadex (A-50) column chromatography and gel filtration of sephadex G-200. The enzyme was purified about 380 fold with 25 ％ recovery.