• BMB Reports
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• v.35 no.6
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• pp.576-582
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• 2002

Collagenase from the internal organs of a mackerel was purified using acetone precipitation, ion-exchange chromatography on a DEAE-Sephadex A-50, gel filtration chromatography on a Sephadex G-100, ion-exchange chromatography on DEAE-Sephacel, and gel filtration chromatography on a Sephadex G-75 column. The molecular mass of the purified enzyme was estimated to be 14.8 kDa by gel filtration and SDS-PAGE. The purification and yield were 39.5-fold and 0.1% when compared to those in the starting-crude extract. The optimum pH and temperature for the enzyme activity were around pH 7.5 and $55^{\circ}C$, respectively. The $K_m$ and $V_{max}$ of the enzyme for collagen Type I were approximately 1.1 mM and 2,343 U, respectively. The purified enzyme was strongly inhibited by $Hg^{2+}$, $Zn^{2+}$, PMSF, TLCK, and the soybean-trypsin inhibitor.

• Journal of Food Hygiene and Safety
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• v.14 no.3
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• pp.233-237
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• 1999

The bacteriocin produced by Lactobacillus sp. GM7311 was purified by sequential steps including n-propanol/acetone treatment, CM-cellulose chromatography, and gel filtration on Sephacryl HR-100. The relative activity of bacteriocin increased 493-fold after final purification step with a recovery of 8.3%. Two protein bands of ca. 8,200 and 2,500 were detected by SDSPAGE of bacteriocin purified through CM-cellulose and sephacryl HR-100 chromatography and both of them had bacteriocin activity.

• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.4
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• pp.587-593
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• 1995

Lectin was purified by using $(NH_4)_2SO_4$, DEAE-cellulose ion-exchange chromatography and Sephadex G-150 column chromatography from Alismatis Rhizoma(AR). The specific activity of AR lectin was 50, 441units/mg, and purification folds were 114. The AR lectin agglutinated human erythrocytes of all types(A, B, O, AB). The molecular weight of AR lectin was estimated about 90, 500 daltons by gel filtration and each subunits were 42,000, 27,000 and 22,500 daltons on SDS-PAGE respectively. The hemagglutinating activity of the lectin was inhibited by sialic acid, glucose, ribose, galactose, sucrose, and lactose. It was also inhibited by cations such as $Hg^{++},\;Fe^{++},\;Cu^{++}\;and\;Pb^{++}$.

• Microbiology and Biotechnology Letters
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• v.13 no.3
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• pp.185-189
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• 1985

Extracellular $\beta$-galactosidase from the culture broth of L. sporogenes was purified to apparent homogeniety by procedures including ammonium sulfate fractionation, Sephadex G-200 gel filtration, DEAE-Sephadex A-50 ion exchange chromatography, and Hydroxyapatite adsorption chromatography. The purifying procedures resulted in 347-fold purification with the overall yield of 39.5％ The purified enzyme had a specific activity(using ONPG as a substrate) of about 1, 585 units per mg protein. The molecular weight of the enzyme protein was estimated to be 140, 000 by gel filtration on Sephadex G-200, and SDS-polyacrylamide gel electorphoresis showed that the enzyme consisted of two identical subunits with a molecular weight of 72, 000.

• Korean Journal of Microbiology
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• v.29 no.2
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• pp.92-96
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• 1991

The soluble cytochrome c-551 of photosynthetic bacterium, Rhodopseudomonas gelatinosa ATCC 17013 was purified through a sequene of four step chromatography including CM-cellulose ion-exchange chromatography, DEAE-Sephacel chromatography, Sephacryl s-200 gel permeation chromatography, and HPLC (SP-5PW). The molecular weight of the purified cytochrome c-551 was 14, 600 Da, and this protein shows the absorption peak at 551 nm, 522 nm, and 417 nm as the reduced form, and at 412 nm as the oxidized form. The cytochrome c-551 seems to be a substrate for the terminal oxidase in the electron transport chain.

• Journal of the Korean Chemical Society
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• v.41 no.11
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• pp.612-638
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• 1997

The methods of separation and recovery of rare earth elements in monazite sand have been studied by the ion exchange chromatography. Both of cation and anion exchange resin were used as ion exchange resins and the solutions of EDTA, DTPA, IMDA and Ln-EDTA were used as eluents. The H+, Zn2+, Fe3+, Al3+, Cu2+, and NH4+ forms of cation exchange resin were used as retaining ions. Ln-EDTA solution was loaded on the EDTA form of anion exchange resin and separated. The Ln-EDTA solution was also used as an eluent for a selective separation of one element from the rare earth mixture solution. The size effects of resin column, the elution mechanism for the various elution types and the separation of a large amount of rare earths were studied.

• Korean Journal of Pharmacognosy
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• v.24 no.2
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• pp.177-182
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• 1993

The pericarp of Cornus officinalis is well known famous medicinal drug in oriental countries. In this work, we have tried to evaluate the toxicity and also to find the lectin components from this seed. The lyophilized seed extract was lethal to experimental mouse at $250{\sim}300mg/kg$ and this toxic components were related to proteins. The lectins components were partially purified from the extract by ion exchange column chromatography. These lectins were relatively stable at temperature variations and also stable at pH $4{\sim}7$. The activity of these lectins did not inhibit by common carbohydrates molecules.

• Microbiology and Biotechnology Letters
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• v.15 no.6
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• pp.420-424
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• 1987

Isocitrate lyase from crude extract of Saccharomycopsis lipolytica ATCC44601 and MX9-11RX8 temperature-sensitive mutant was purified about 54 times and 87 times, respectively by ammonium sulfate fractionation, Toyo peal HW-55F gel filtration and DEAE-Cellulose ion exchange chromatography, The molecular weight of the purified isocitrate lyase from this yeast was estimated to be 230, 000 by gel filtration on Sephadex G-200, and SDS-polyacrylamide Eel electrophoresis showed that the enzyme consisted of four identical or similar subunits with a molecular weight of 59, 000 and the enzyme showed optimum activity at pH 6.9.

• Journal of Life Science
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• v.6 no.2
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• pp.120-128
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• 1996

In the screening of actinomycetes culture filtrate for inhibitor of adenosine deaminase, a novel inhibitor was found in a cultured broth of strain J-144K. The optimum conditions for the adenosine deaminase inhibitor production from the isolated strain J-144K were evaluated. This strain showed the maximum yield of adenosine deaminase inhibitor when grown at pH 7.0 and 30$\circ$C for 60 hours in the medium of 1.0% dextrose, 0.5% yeast extract, 0.5% peptone and 0.1% KH$_{2}$PO$_{4}$ under the aerobic condition. Through the activated charcoal extraction, methanol fractionation, Dowex 50 H$^{+}$ X-8 ion exchange column chromatography, Dowex CI$^{-}$ X-8 ion exchange column chromatography, and Sephadex G-15 gel filtration procedures, this inhibitor was purified with three materials.

• The Korean Journal of Zoology
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• v.34 no.2
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• pp.196-202
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• 1991

Juvenile honnone binding protein (JHBP) was identified in the last instar larval hemolymph of Lymantria dispar using dextran coated charcoal (DCC) binding assay and gel filtration. The p1 value of JHBP was estimated to be 5.3. JHBP was partially pudfied by polyethylene glycol(PEG) precipitation, DEAE-cellulose ion-exchange chromatography and gel filtration, and was confirmed by DCC binding assay.