• KOREAN JOURNAL OF CROP SCIENCE
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• v.38 no.4
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• pp.350-359
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• 1993

The effect of gibberellic acid ($GA_3) and abscisic acid (ABA) on KCl-enhanced proteolysis of senescing leaves of rice(Oryza sativa L. cv. Chilsung) was studied. Emphasis was given to their effects on KCI-enhanced efflux of amino acids and proteinase activity. When treated singly, $GA_3 affected leaf proteolysis little, while ABA increased proteolysis, the rate of amino acid efflux, and ribulose -1,5 -bisphosphate carboxylase / oxygenase (Rubisco)-degrading endoproteinase activity. An additive increase in all three parameters mentioned above was observed when leaves were treated with ABA and KCl. No such an additive effect was found when $GA_3 was treated with KCl. Both $GA_3 and ABA helped to alleviate the KCI-suppressed activity of Rubisco-degrading exoproteinases. The additive increase in proteolysis of rice leaves in the presence of both ABA and KCl could thus be ascribed to a further increase in the efflux of protein hydrolyzates and Rubisco-degrading endoproteinase activity. An increase in proteolysis was accompanied by a decrease in water absorption, and the combined treatment of ABA with KCl resulted in a further reduction of water absorption.

• Korean Journal of Microbiology
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• v.39 no.4
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• pp.207-215
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• 2003

Gene structure prediction, which is to predict protein coding regions in a given nucleotide sequence, is the most important process in annotating genes and greatly affects gene analysis and genome annotation. As eukaryotic genes have more complicated stuructures in DNA sequences than those of prokaryotic genes, analysis programs for eukaryotic gene structure prediction have more diverse and more complicated computational models. We have developed EGSP, a eukaryotic gene structure program, using duration hidden markov model. The program consists of two major processes, one of which is a training process to produce parameter values from training data sets and the other of which is to predict protein coding regions based on the parameter values. The program predicts multiple genes rather than a single gene from a DNA sequence. A few computational models were implemented to detect signal pattern and their scanning efficiency was tested. Prediction performance was calculated and was compared with those of a few commonly used programs, GenScan, GeneID and Morgan based on a few criteria. The results show that the program can be practically used as a stand-alone program and a module in a system. For gene prediction of eukaryotic microbial genomes, training and prediction analysis was done with Saccharomyces chromosomes and the result shows the program is currently practically applicable to real eukaryotic microbial genomes.

• Proceedings of the KIEE Conference
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• 2007.07a
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• pp.280-281
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• 2007

본 논문에서는 생체 내에 삽입하거나 연속적으로 혈당을 모니터링하기 위하여 제작된 무효소 혈당세서의 바이오 패키징 및 특성 최적화에 관하여 고찰하였다. 3전극을 갖는 동일한 센서구조에서 sensitivity를 최대화하기 위해 평면형 백금전극을 사용한 센서, 메조포러스 구조가 작동전극에 형성된 센서, 메조포러스 구조가 작동전극과 보조전극에 형성된 무효소 혈당센서를 설계, 제작하고 비교하였다. 각각의 센서는 0.009${\mu}A$ $mM^{-1}cm^{-2}$, 5.46${\mu}A$ $mM^{-1}cm^{-2}$, 7.75${\mu}A$ $mM^{-1}cm^{-2}$의 sensitivity를 가졌다. 또한 생체 이식되었을 때 혈액 속에서 글루코스응답을 얻는 데에 있어 방해종인 Ascrobic Acid와 Acetaminophen의 반응을 최소화하고, 혈액 내의 단백질들이 전극에 엉겨 붙는 것을 막기 위해 생체 적합한 물질인 Nafion 을 패키징 멤브레인으로 적용하여 센서를 제작하였다. 이 센서는 0.36${\mu}A$ $mM^{-1}cm^{-2}$의 sensitivity를 가졌다.

• Korean Journal of Food Science and Technology
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• v.21 no.3
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• pp.338-344
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• 1989

This study was conducted to investigate the mechanism involved with gelation of soybean proteins, 7S and 11S. For the preparations of soybean gels, calsium coagulation and isoelectric point precipitation through the lactic acid fermentation were employed. The textural properties and microstructure of soybean curds were examined by Instron Universal Testing Machine and Scanning Electron Microscope(SEM), respectively. Soybean cheeses were also prepared from soyprotein curds. The characteristics of prepared soybean cheeses were studied by Instron and Sensory evaluation. Microstructure of soybean curds demonstrated by SEM differed markely, postulating that molecular interaction occured in the curds varied with type of protein and coagulative conditions. Textural parameter measured by Instron demonstrated that the curds and the cheeses made through lactic acid fermentation showed higher values in hardness, gumminess and chewiness than those coagulated with $CaCl_2$ 11S PRF could give the curds with higher values in hardness, cohesiveness, springiness, gumminess and chewiness than SPI and 7S PRF Sensory evaluation results showed that soybean cheese made from 11S PRF scored higher values in taste, chewiness, and hardness. However, panels preferred soybean cheese prepared from SPI in color, chewiness and brittleness.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2004.10a
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• pp.1-29
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• 2004

본 연구에서 저알레르기 처리 공정은 Autoclaving, 가열처리, micro wave, dry heating, 초음파, 효소, 인산염, 천연효소, 가용화, 복합처리 등의 처리 공정으로 하였다. 저 allergy처리에서 allergy가 완전히 억제되는 것은 가열처리를 한 것으로 쇄양 B(추출액+가열 3분), autoclave 처리, micro파 처리, dry heating처리, 복합처리를 했을 때이다. 또한 천연효소(키위)를 침지한 후 tolergen과 같이 3분간 가열했을 때 allergy가 억제되는 것으로 나타났다. 즉 가열처리로 인한 단백질 구조 변성으로 이러한 결과를 보인 것으로 보인다. 인산염의 경우도 어느 정도 억제가 되는 것으로 보이고 있다. 나머지 처리들은 거의 효과를 보이고 있지 않다. 천연효소와 tolergen(쇄양)을 그냥 처리했을 때에는 allergy 억제효과는 없는 것으로 나타났다. 우유의 저 allergy 처리는 효소, autoclave, micro 파, NaOH 처리, 복합처리에서 감소되는 것으로 나타났다. 이러한 결과는 western blotting으로도 확인되었으며 그 억제율 %은 식육에서는 상당한 가열처리를 통하여 알레르기를 감소시킬 수 있는 것을 볼 수 있으며 또한 인산염, 가용화(NaOH처리)도 저 알레르기 효과가 있음을 알 수 있다. 키위, 쇄양 단독 처리 시 저 알레르기 효과가 없지만 약간의 가열을 통하여 알레르기가 감소됨을 알 수 있다. 우유는 효소나 autoclave 처리만이 저 allergy 효과가 각각 28%, 45%로 적게 나타났다. 모든 복합처리의 경우에서는 그 억제율이 41-96%로 높은 효과가 있음을 알 수 있다. 천연효소처리와 인산염 처리된 식육의 전자현미경적 관찰은 control과 비교시 조직의 변화가 없고 둘다 근육 단백질 구조를 분산시키는 것으로 나타났다. 또한 고기를 단계별 복합처리로 저 allergy 처리는 단계별로 점차적으로 allergy가 감소되었다. 즉 단계별로 억제가 안되는 것부터 억제되는 처리를 복합적으로 처리한 것으로 그 단계는 천연효소처리에 인산염 처리, 여기에 초음파 처리, 마지막 단계로 3분 끓이면 억제율이 68%까지 억제되었다. 이는 단일처리시 전혀 억제를 못하는 처리를 단계별로 한 단계씩 더해가면 allergy 억제효과가 나타난다고 할 수 있겠다. 초음파 처리도 역시 저 allergy 처리 공정에 이용될 수 있는데 이것은 그 처리로 인해 새로운 알러젠이 생성될 수도 있다. 또한 복합처리로 allergy를 감소시키면 연속적이고 동시적으로 하기 때문에 원가를 절감할 수 있다.

• Korean journal of applied entomology
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• v.34 no.2
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• pp.112-119
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• 1995

Anatomical and biochemical changes of the corn root injured by the root lesion nematode, Pratylenchus vulnus, were examined to understand the interactions between the nematode and the crop which can be applied to a breeding program for nematode-resistant crop. The nematode and the crop which can be applied to be a breeding program for nematode-resistant crop. The nematode entered the cortex of corn root through its epidemis. They moved to other cortical cells by breaking their cell walls. They, finally, gathered around the endodermis of the roots and the bases of the root hairs. Parasitism of the nematode formed cavities within the root tissues where the females laid eggs. Major root damage by the nematode occurred in the cortical cells where must cell walls were broken and crushed to form empty spaces. These empty spaces in the base of the root resulted in this breakdown. Damage-induced biochemical changes of the corn roots were analysed by their total protein patterns and esterase activities in both control and nematode-infected roots. Denaturing gel did not show any significant difference in the banding patterns between them. Esterase patterns and activities, also, were not significantly different between the infected and the control roots.

• Restorative Dentistry and Endodontics
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• v.35 no.3
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• pp.211-221
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• 2010

Proteoglycan is highly hydrophilic and negatively charged which enable them attract the water. The objective of study was to investigate the effects of Proteoglycan on microtensile bond strength of dentin adhesives and on architecture of dentin collagen matrix of acid etched dentin by removing the chondroitin sulphate attached on Proteoglycan. A flat dentin surface in mid-coronal portion of tooth was prepared. After acid etching, half of the specimens were immersed in 0.1 U/mL chondroitinase ABC (C-ABC) for 48 h at $37^{\circ}C$, while the other half were stored in distilled water. Specimens were bonded with the dentin adhesive using three different bonding techniques (wet, dry and re-wet) followed by microtensile bond strength test. SEM examination was done with debonded specimen, resin-dentin interface and acid-etched dentin surface with/without C-ABC treatment. For the subgroups using wet-bonding or dry-bonding technique, microtensile bond strength showed no significant difference after C-ABC treatment (p > 0.05). Nevertheless, the subgroup using rewetting technique after air dry in the Single Bond 2 group demonstrated a significant decrease of microtensile bond strength after C-ABC treatment. Collagen architecture is loosely packed and some fibrils are aggregated together and relatively collapsed compared with normal acid-etched wet dentin after C-ABC treatment. Further studies are necessary for the contribution to the collagen architecture of noncollagenous protein under the various clinical situations and several dentin conditioners and are also needed about long-term effect on bond strength of dentin adhesive.

• Journal of Life Science
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• v.6 no.4
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• pp.304-312
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• 1996

In the present report, a p[ossibility of the interaction fo Ser-33 and Asp-112 residues in folding of tryptophan synthase $\alpha$ subunit was explored by examining the effect of single or double substitution of these residues on folding of $\alpha$ subunit in E. coli. $\alpha$ subunit of which Ser-33 was substituted with Leu (SL33) was accumulated as insoluble aggregate form, when overproduced in E. coli, whereas $\alpha$ subunit of which Asp-112 was replaced by Asn (DN112) or Gly (DG112) was accumulated as soluble form to the similar extent as wild type $\alpha$ subunit was. When these alterations were combined into one protein, the synergistic effect of residues 33 and 112 on the amount of aggregate form was shown. The amount of doubly altered SL33/DG112 $\alpha$ subunit as aggregate form was increased 5-13 fold that of SL33 $\alpha$ subunit, and the amount of SL33/DG112 $\alpha$ subunit as aggregate form was decreased 3-4 fold that of SL33 $\alpha$ subunit. Aggregates are derived from the specific association of partially folded or unassembled subunits in the folding process. Therefore, this result suggests that residues 33 and 112 of $\alpha$ subunit may unteract during the folding of this enzyme in E. coli.

• Korean Journal of Microbiology
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• v.52 no.3
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• pp.278-285
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• 2016

The bifunctional PheA protein, having chorismate mutase and prephenate dehydratase (CMPD) activities, is one of the key regulatory enzymes in the aromatic amino acid biosynthesis in Escherichia coli, and is negatively regulated by an end-product, phenyalanine. Therefore, PheA protein has been thought as useful for protein engineering to utilize mass production of essential amino acid phenylalanine. To obtain feedback resistant PheA protein against phenylalanine, we mutated by using random mutagenesis, extensively screened, and obtained $pheA^{FBR}$ gene encoding a feedback resistant PheA protein. The mutant PheA protein contains substitution of Leu to Phe at the position of 118, displaying that higher affinity (about $290{\mu}M$) for prephenate in comparison with that (about $850{\mu}M$) of wild type PheA protein. Kinetic analysis showed that the saturation curve of $PheA^{FBR}$ against phenyalanine is hyperbolic rather than that of $PheA^{WT}$, which is sigmoidal, indicating that the L118F mutant enzyme has no cooperative effects in prephenate binding in the presence of phenylalanine. In vitro enzymatic assay showed that the mutant protein exhibited increased activity by above 3.5 folds compared to the wild type enzyme. Moreover, L118F mutant protein appeared insensitive to feedback inhibition with keeping 40% of enzymatic activity even in the presence of 10 mM phenylalanine at which the activity of wild type $PheA^{WT}$ was not observed. The substitution of Leu to Phe in CMPD may induce significant conformational change for this enzyme to acquire feedback resistance to end-product of the pathway by modulating kinetic properties.

• Korean Journal of Microbiology
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• v.38 no.3
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• pp.153-161
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• 2002

Sox4, a transcription factor, consists of three functional domains: an HMG-box domain as a DNA binding domain, serine rich region as a transactivation domain and glycine rich region (GRR), an unknown functional domain. Although Sox4 is known to be functionally involved in heart, B-cell and reproductive system development, its physiological function remains to be elucidated. We used pGEX expression system to develop a simple and rapid method for purifying Sox4 protein in suitable forms for biochemical studies of their functions. Unexpectedly, we observed that full-length Sox4 appears to be protease-sensitive during expression and purification in E. coli. To map the protease-sensitive site in Sox4, we generated various constructs with each of functional domains of Sox4 and purified as the GST-Sox4 fusion proteins using glutathione beads. We found that the specific cleavage site for the proteolytic enzyme, which exists in E. coli, is localized within the novel GRR of Sox4. Our study suggest that the GRR of Sox4 may a target for the cellular protease action and this cleavage in the GRR may be involved in regulating physiological function of Sox4. Additionally, our study may provide a useful method for investigating the proteolytic cleavage of the target molecule in E. coli.