• Food Science of Animal Resources
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• v.29 no.2
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• pp.164-167
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• 2009

The lactoferrin from mongolian mare colostrum has been purified by gel filtration (Sephadex G-100), affinity chromatography (Toyopear1-AF-Heparin-650M) in two steps. Mare lactoferrin-containing fractions were identified in the first peak among 3 peaks on Sephadex G-100 as first step, and purified lactoferrin was eluted with a step gradient of 0.5M NaCl as a 3 step (gradient 0.1,0.3, 0.5M). Eluted fractions were analyzed by 12% SDS-PAGE, and showed a single protein. Its molecular weight was estimated to be 82kDa. N-terminal amino acid sequence was determined as APRKSVRWCTISPAEXAKXA.

• Journal of Life Science
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• v.9 no.1
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• pp.45-49
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• 1999

Seaweed alginate was acetylated by activated carbon immobilized Pseudomonas syringae in a fluidized bed, up-flow reactor. The acetylation degree of seaweed alginate was about 30%. Calcium-acetylated seaweed alginate gel bead was made and compared to calcium-seaweed alginate gel bead by the scanning electron microscopy (SEM). Structural difference of two gel beads may results from increased viscosity and decreased affinity of acetylated seaweed alginate for calcium ion. On the basis of interior and exterior structure of calcium-acetylated seaweed alginate gels and property of acetylated seaweed alginate, it seems that acetylated seaweed alginate is used for the supporter for electrophoresis and packing materials for liquid chromatography and gel filtration.

• The Journal of Natural Sciences
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• v.8 no.1
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• pp.41-45
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• 1995

A. partially decationized Y zeolite was pretreated under specific conditions. It was found this calcinated zeolite retains its separation properties for mixtures of the gases hydrogen, nitrogen, oxygen, carbon monoxide, and methane but has much lower affinity for water molecules than untreated, e.g., zeolites A type or X type. The observed effect is discussed on the basis of the results of adsorption measurements on the adsorption capacities, isotherms, and heats of adsorption.

• Molecules and Cells
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• v.20 no.2
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• pp.297-302
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• 2005

The integrity and proper functioning of telomeres require association of telomeric DNA sequences with specific binding proteins. We have characterized PLP-1, a $PUR{\alpha}$ homolog encoded by F45E4.2, which we previously identified as a candidate double stranded telomere binding protein, by affinity chromatography followed by mass spectrometry. PLP-1 bound double-stranded telomeric DNA in vitro as shown by competition assays. Core binding was provided by the third and fourth nucleotides of the TTAGGC telomeric repeat. This is quite different from the binding sequence of CEH-37, another C. elegans telomere binding protein, suggesting that multiple proteins may bind nematode telomeric DNA simultaneously in vivo.

• Molecules and Cells
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• v.24 no.2
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• pp.268-275
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• 2007

Protein phosphorylation plays a key role in signal transduction in cells. Since phosphoproteins are present in low abundance, enrichment methods are required for their purification and analysis. Chemical derivatization strategies have been devised for enriching phosphoproteins and phosphopeptides. In this report, we employed a strategy that replaces the phosphate moieties on serine and threonine residues with a biotin-containing tag via a series of chemical reactions. Ribulose 1,5-bisphosphate carboxylase/oxygenase (RUBISCO)-depleted protein extracts prepared from Arabidopsis seedlings were chemically modified for 'biotin-tagging'. The biotinylated (previously phosphorylated) proteins were then selectively isolated by avidin-biotin affinity chromatography, followed by two-dimensional gel electrophoresis (2-DE) and matrix-assisted laser-desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS). This led to the identification of 31 protein spots, representing 18 different proteins, which are implicated in a variety of cellular processes. Despite its current technical limitations, with further improvements in tools and techniques this strategy may be developed into a useful approach.

• Proceedings of the Membrane Society of Korea Conference
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• 1991.10a
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• pp.45-46
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• 1991

분리막 공정은 상변화를 일으키지 않기 때문에 장치비가 저렴하며, 열 및 화학적으로 민감한 물질, 특히 생체물질 등을 다루는데 적합하다. 또한 최종 생성물질을 정제하는 방법으로는 이온교환 크로마토그래피, 전기 영동 및 친화성 크로마토그래피(affinity chromatography)가 있다. 이중 친화성 크로마토그래피는 가장 선택적이고, 단일 장치로서 기존의 분리방법에 비해 약 1000배 가까이 정제할 수 있다. 본 실험에서는 트립신 억제제인 m-aminobenzamidine을 포함하고 있는 수용성 고분자를 제조하여 트립신을 선택적으로 분리하고자 하였으며, 본 연구 필요한 분리막은 막제조가 용이하며 비용이 저렴한 cellulose acetate막을 사용하였다. CA 막의 세공크기는 겔화매질의 에탄올 농도로 조절하였다. Casting 용액의 조성은 다음 표에 간략하게 나타내었다.

• Microbiology and Biotechnology Letters
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• v.24 no.4
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• pp.445-451
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• 1996

The strain YCH-37, which produces yeast cell wall lytlc enzyme, was isolated from soil. From the microscopic observation, morphological and cultural characteristics, this strain was identified to fungus, Dicyma sp. So, we named this strain as Dicyma sp. YCH-37. The lytic enzyme effectively lysed Salmonella typhimurium among intact living bacteria and Torulopsis, Hansenula, Zygosaccharomyces among intact living yeast, as well as autoclaved yeast strains. The yeast cell wall lytic enzyme was succesively purified to 204 folds with 13% yields through yeast glucan affinity adsorption and DEAE-cellulose column chromatography. The enzyme was identified to monomeric protein with molecular weight of 25,000 daltons from the results of SDS-PAGE and gel filtration. The optimum pH and temperature for the yeast lytic activity were 8.0 and 50$\circ$C, respectively. The enzyme was stable up to 40$\circ$C, and between pH 4.0-pH 10.0.

• Preventive Nutrition and Food Science
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• v.4 no.2
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• pp.139-144
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• 1999

Lipoprotein lipase (LPL) I san enzyme that catalyzed the hydrolysis of triacylglycerols of chylomicrons and VLDL to produce 20acylglycerols and fatty acids. The enzyme, LPL, is localized on the surface of the capillary endothelium and is widely distributed in extrahepatic tissues including heart, skeletal muscle and adipose tissue. LPL has been isolated from boving milk by affinity chromatography on heparin-separose in 2 M NaCL, 5mM barbital buffer, pH 7.4. To elucidate the lipid-binding regin, LPL was digested with trypsin and then separated by gel filtration. Lipid binding region of LPL has been investigated by recombining LPL peptides with DMPC vesicles. Proteolytic LPL fragments with DMPC were reassembled and stabilized by cholate. Lipid-binding region of LPL was identified by a PTH-automated protein sequencer, as AQQHYPVSAGYTK. The analysis of the secondary structure of the lipid-binding peptides revealed a higher probability of $\alpha$-helix structure compared to the whole LPL protein. The prediction of hydrophobicity of lipid -binding region was highly hydrophobic (-1.1) compared to LPL polypetide(-0.4).

• YAKHAK HOEJI
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• v.46 no.4
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• pp.270-275
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• 2002

The lectin gene from rice was amplified by the polymerase chain reaction. The amplified DNA was inserted into the expression vector pET26b and expressed it as a fusion protein with polyhistidine sequences in Escherichia coli. The recombinant protein was produced by induction with 0.4 mM isopropyl-$\beta$-D-thiogalactopyranoside at 37$^{\circ}C$ and purified by an immobilized metal affinity chromatography. The recombinant protein was found to have lectin activity by the hemagglutination inhibition assay. The hemagglutination activity of the recombinant protein was optimal at pH 4.0-7.0 and was dependent on $Ca^{2+}$ and Mn$^{2+}$.2+/.

• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.3
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• pp.389-395
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• 1995

The neutral sugar sidechains of apple pectins were hydrolyzed by commercial hemicellulase produced from Aspergillus niger, and the corresponding changes in solution viscosity were investigated in dilute(cc*) pectin solutions. Pectinase activity included in hemicellulases was removed by Epoxy-activated Sepharose 6B affinity chromatography using polygalacturonic acid as a ligand. Enzymatic hydrolysis of sidechains did not affect the specifc viscosity of dilute(0.5%) pectin solutions, while viscosity significantly decreased in concentrated(2.0∼6.0%) region. These results strongly suggest that the sidechains of pectins exists as an entangled state in concentrated solutions. It was also found that in the concentrated region the extent of viscosity reduction was dependent on pectin concentrations.