• Animal cells and systems
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• v.1 no.1
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• pp.135-142
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• 1997

Random sequencing of expressed sequence tags in roots of Chinese cabbage led to isolation of a partial cDNA clone, BR77, which encoded a putative protein kinase. Using the BR77 cDNA as a probe, we isolated a full-length cDNA encoding the Brassica campestris protein kinase 1 (Bcpk1). The Bcpt1 cDNA contained one open reading frame encoding a polypeptide of 439 amino acids. The putative polypeptide consisted of a short N-terminal region and a protein kinase catalytic domain. The catalytic domain of Bcpkl showed a high homology to cAMP- and calcium- phospholipid-dependent subfamilies of serine/threonine protein kineses. Eleven major catalytic domains in protein kineses were well conserved in Bcpk1. However, Bcpk1 contained a unique nonhomologous intervening sequence between subdomains VII and VIII, which was not found in protein kineses of animals and lower eukaryotes. Genomic DNA gel blot analysis showed that Bcpt1 genes might be present as three copies in the Chinese cabbage genome. These imply that Bcpk1 belongs to a plant-specific serine/threonine protein kinase subfamily.

• Journal of Microbiology
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• v.44 no.2
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• pp.145-154
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• 2006

Heterotrimeric G proteins (G proteins) are conserved in all eukaryotes and are crucial components sensing and relaying external cues into the cells to elicit appropriate physiological and biochemical responses. Basic units of the heterotrimeric G protein signaling system include a G protein-coupled receptor (GPCR), a G protein composed of ${\alpha},\;{\beta},\;and\;{\gamma}$ subunits, and variety of effectors. Sequential sensitization and activation of these G protein elements translates external signals into gene expression changes, resulting in appropriate cellular behaviors. Regulators of G protein signaling (RGSs) constitute a crucial element of appropriate control of the intensity and duration of G protein signaling. For the past decade, G protein signaling and its regulation have been intensively studied in a number of model and/or pathogenic fungi and outcomes of the studies provided better understanding on the upstream regulation of vegetative growth, mating, development, virulence/pathogenicity establishment, and biosynthesis of secondary metabolites in fungi. This review focuses on the characteristics of the basic upstream G protein components and RGS proteins, and their roles controlling various aspects of biological processes in the model filamentous ascomycete fungus Aspergillus nidulans. In particular, their functions in controlling hyphal proliferation, asexual spore formation, sexual fruiting, and the mycotoxin sterigmatocystin production are discussed.

• Journal of the East Asian Society of Dietary Life
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• v.7 no.2
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• pp.153-158
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• 1997

This study was designed to find out the effects of soybean protein and milk protein between nondiabetic and diabetic rats. The experimental results are summarized as follows. 1. Total food intake was higher in diabetic soybean protein group than other groups but it was not significant. 2. The change of body weight was lower in diabetic soybean protein group than other groups and the soybean protein was effective to maintain the ideal body weight. 3. The effects of lowering total cholesterol and glucose in serum was higher in soybean protein groups than the milk protein groups.

• Korean Journal of Microbiology
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• v.28 no.3
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• pp.258-263
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• 1990

A cadmium-binding protein was purified the cell-free extract of extreme cadmium tolerant Hansenula anomala B-7. The molecular weight was determined to be approximately 33, 000 and was composed two kinds of subunits having a molecular weight of 18, 000 and 14, 000, respectively. The extinction coefficient of the cadmium-binding protein was calculated to be 19.58. The amount of cadmium in the cadmium-binding protein was $9.26{\mu}{\textrm{g}}$ per $100{\mu}{\textrm{g}}$ of protein. A total of 14 amino acids were detected in the cadmium-binding protein, including aspartic acid, glycine and alanine that were present in a high quantity, but proline, valine and methionine were not found. The purified cadmium-binding protein contained a high quantity of cysteine and cadmium, and therefore this protein showed clearly the characteristics of metallothionein.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.6
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• pp.758-762
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• 1993

The effect of sodium hexametaphosphate(SHMP) on the extraction of defatted sesame meal protein and the color and amino acid composition of protein concentrate have been studied. The highest amount of protein could be extracted with 1.5% SHMP and the extraction was effective at pH 12.0. The extraction rate tended to increase with increasing the flour to solvent ratio and about 60% of protein was obtained when adjusted the ratio to 1 : 40. Color of sesame protein concentrate was slightly improved by SHMP treatment. Lysine and methionine content were decreased in SHMP-treated protein concentrate but valine and leucine content were increased.

• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.4
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• pp.619-624
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• 1995

Sesame protein concentrate(SPC) was prepared from defatted sesame flour(DSF) at several different pH(2.0, 7.0, 9.0, 11.0) for protein extraction. Some of their functional properties were determined in order to compare the effects of pH during preparation of concentrates. Compared with DSF, nitrogen solubility was markedly improved in all SPC, and SPC extracted at pH 11.0 showed the highest solubility at all pH leaves examined. Fatabsorption was increased in all SPC prepared, but water absorption was decreased as the extraction pH of protein increased. The emulsifying properteis and foaming properties of SPC were remarkably higher than DSF. As the extraction pH of protein was increased, the emulsion activity was also increased, but emulsion stability was decreased. SPC extracted at pH 7.0 showed the highest foaming capacity on the other hand, the highest foaming stability was shown in SPC extracted at pH 2.0. As the protein extraction pH increased, the viscosity of the protein solution was increased. SPC extracted at pH 11.0 showed highest viscosity at all protein concentrations tested.

• Proceeding of EDISON Challenge
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• 2016.03a
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• pp.90-95
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• 2016

Heat Shock 70kDa Protein 1-Like(HSPA1L)는 Heat-shock protein70(HSP70) family에 속하는 chaperone protein으로 polypeptide folding, assembly, protein degradation 등 다양한 biological processes에 관여하고 있다. HSPA1L은 human methyltransferase-like protein 21A(METTL21A)에 의해 lysine residue에 methylation이 일어나게 되는데, 암세포에서 일반적인 HSPA1L은 주로 세포질에서 발견되는 반면 methylated HSPA1L의 경우 주로 핵에서 발견이 됨으로써 HSPA1L methylation이 암 세포 성장에 중요할 역할을 할 것이라 추측되며 anti-cancer drug target으로 주목 받고 있다. 하지만 현재 HSPA1L의 구조가 부분적으로만 밝혀져 있어 HSPA1L와 METTL21A가 어떤 residue들이 interaction 하여 binding을 하는지에 대해서 아직 밝혀 지지 않았다. 이로 인해 anti-cancer drug target으로서의 연구에 제한이 있다. 이번 연구에서는 homology modeling(Galaxy-TBM, Galaxy-refine)을 통해 HSPA1L 전체 구조를 밝혀 낸 후, HSPA1L 와 METTL21A를 protein-protein docking을 통해 binding pose 예측을 하였다. 이러한 binding pose를 protein interaction analysis하여 HSPA1L과 METTL21A binding에 관여하는 중요 residue들을 밝혀 냈다. 이러한 structural information은 methylated HSPA1L와 암 세포 성장간의 연관성, 더 나아가 anti-cancer drug 개발로 까지도 이어 질 수 있을 것이라 생각한다.

• Journal of the Korean Magnetic Resonance Society
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• v.23 no.4
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• pp.104-107
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• 2019

Many proteins are expressed as an insoluble form during the production using Escherichia coli (E. coli) system. Although various methods are applied to increase their amounts of soluble expression, refolding is the only feasible way to obtain a target protein in some cases. Moreover, protein NMR experiments require ¹³C/¹⁵N-labeled proteins that can only be obtained from E. coli systems in terms of cost and technical difficulty. The finding of appropriate refolding conditions for a target protein is a time-consuming process. In particular, it is very difficult to determine whether the refolded protein has a native structure, when a target protein has no enzymatic activity and its refolding yield is very low. Here, we showed that 1-dimensional ¹H-¹⁵N heteronuclear single quantum correlation (1D ¹H-¹⁵N HSQC) experiment can be efficiently used to screen an optimal condition for the refolding of a target protein by monitoring both the structure and concentration of the refolded protein.

• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.1
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• pp.41-47
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• 1995

This experiments was designed to evaluated the chemical components and nutrition of Aspergillus fumigatus cells. This dried fungal mycellia was consist of crude protein 48.5%, crude lipid 2.9%, carbohydrate 44.7% and total ash 3.4%, respectively. The major fatty acid of total lipid were 27.9% of linoleic acid, 24.6% of oleic acid, 15.4% of palmitic acid and 10.6% of linolenic aicd. Amino acid analysis indicated that the protein was rich in aspartic acid, glutamic acid, leucine, lysine but poor in cystein, methionine, histidine. The fungal cake of Aspergillus fumigatus, when dried and specially processed, has been found to serve as a source of protein in place of soybean meal in the diet of experimental mice. Animal were fed a control diet first, and an incease in weight proved the formulation to be satisfactory. At the end of a 30-day period, the experimental mice showed increases in weight comparable to those of the control animals. The net protein efficiency ratio for the control diet was 3.42$\pm$0.15 and the fungal protein and succinylated fungal protein with DL-methionine they were 3.12$\pm$0.39 and 2.98$\pm$0.06 respectively. This supports the view that dried and succinylated fungal protein can be substituted as a protein source.

• Animal cells and systems
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• v.7 no.1
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• pp.81-87
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• 2003

While screening proteins that interact with DnaA protein, the initiator protein for Escherichia coil chromosomal DNA replication, we found a 52-kD sized protein which bound to DnaA protein in a salt-dependent manner. This protein was identified as trigger factor, a ribosome-associated peptidyl-prolyl- cisltrans isomerase with chaperone activity. Trigger factor was overproduced and purified to near homogeneity, and its effect on the function of DnaA protein was examined, Enhanced binding of DnaA protein to DnaA box with no apparent supershift in the gel-shift experiments suggested that trigger factor, by virtue of its chaperone activity, exerts a change on DnaA protein thus increasing its binding affinity for DnaA box.