• Tuberculosis and Respiratory Diseases
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• v.50 no.4
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• pp.426-436
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• 2001

Background : Chronic obstructive pulmonary disease(COPD) is one of the major contributors to morbidity and mortality among the adult population. Cigarette smoking(CS) is undoubtedly the single most important factor in the pathogenesis of COPD. However, its mechanism is unclear. The current hypothesis regarding the pathogenesis of COPD postulates that an imbalance between proteases and antiproteases leads to the destructive changes in the lung parenchyma. This study had two aims. First, to evaluate the effect of CS exposure on histologic changes of the lung parenchyme, and second, to evaluate the effect of CS exposure on the expression of the gelatinolytic enzymes in BAL fluid cells in guinea pigs. Methods : Two groups of five guinea pigs were exposed to the whole smoke of 20 commercial cigarettes per day, 5 hours/day, 5 days/week, for 6weeks, and 12 weeks, respectively, using a smoking apparatus. Five age-matched guinea pigs exposed to room air were used as controls. Five or more sections were microscopically extamined(${\times}400$) and the number of cellular infiltration of the alveolar wall was measured in order to evaluate the effect of CS exposure on the histologic changes of lung parenchyme. The statistical significance was analyzed by a linear regression method. To evaluate the expression of the gelatinolytic enzymes in intraalveolar cells, BAL fluid was obtained and the intraalveolar cells were separated by centrifugation (500 g for 10 min at $4^{\circ}C$). Two sets of culture plates were loaded with $1{\times}10^6$ intraalveolar cells. One plate, contained O.1mM EDTA, a inhibitor of matrix metalloproteases(MMPs), and the other plate had no EDTA. Both plates were incubated for 48 hours at $37^{\circ}C$. After incubation, gelatinolytic protease expression in the supernatants was analyzed by gelatin zymography. Results : At the end of CS exposure, the level of blood carboxy Hb had increased significantly(4.1g/dl in control group, 24g/dl immediately after CS exposure, 18g/dl 30 min after CS exposure, 15g/dl 1 hour after CS exposure). Alveolar inflammatory cells were identified in the CS exposed guinea pigs. The number of alveolar cellular cells observed in a microscopic field ($400{\times}$) was $121.4{\pm}7.2$, $158.0{\pm}20.2$, $196.8{\pm}32.8$, in the control, the 6 weeks, and the 12 weeks group, respectively. The increased extent of inflammatory cellular infiltration of the lung parenchema showed a statistically significant linear relationship with the duration of CS exposure(p=0.001, $r^2=0.675$). Several types of gelatinolytic enzymes in the intraalveolar cells of CS exposed guinea pigs were expressed, of which some were inhibited by EDT A. However, the gelatinolytic enzymes were not expressed in the control groups. Conclusion : CS exposure increases inflammatory cellular infiltration of the alveolar wall and the expression of gelatinolytic proteases in guinea pigs. EDTA inhibits some of the gelatinolytic proteases. These findings suggest a possibility that CS exposure may increase MMP expression in the lungs of guinea pigs.

• Journal of Nutrition and Health
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• v.2 no.4
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• pp.127-134
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• 1969

Total and esterified cholesterol content was determined in the rat administered animal and vegetable proteins for 16 weeks. The cholesterol biosynthetic activity of the liver was also measured in these rats by the $acetate-C^{14}$ incorporation rate. The results obtained were as follows. (1) Serum total cholesterol content was increased by the administration of animal proteins and decreased by that of vegetable proteins. (2) Liver cholesterol content was increased by animal proteins and decreased by at of vegetable proteins. (3) Cholesterol biosynthetic activity of the liver was increased by the animal proteins and decreased by the vegetable proteins.

• Journal of Veterinary Clinics
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• v.16 no.2
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• pp.328-331
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• 1999

Theileriosis에 대한 효율적인 예방대책을 마련하기 위한 일환으로 발현된 T. sergenti 재조합 항원단백질의 면역원성을 조사하였다. 먼저, E. coli 단백질 발현 vector인 pQE 32 plasmid vector를 이용하여 발현된 T. sergenti의 재조합 막표면단백질(KTs-MP)을 4개월령의 유우 송아지에 접종하였다. 그리고 접종된 송아지의 혈액변화상과 T. sergenti에 대한 항체가의 변화상을 분석한 결과, 재조합단백질의 접종에 의하여 항체가가 상승되는 것을 알 수 있었다. 그러나 재조합단백질의 접종만으로는 T. sergenti의 감염을 완전하게 예방하지는 못하였다.

• Bulletin of Food Technology
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• v.18 no.1
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• pp.3-15
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• 2005

최근 들어 게놈기능연구는 주요국가의 새로운 국가적 연구표적으로 지정되면서 유전자기반 생물산업의 핵심으로 부각되고 있다. 이러한 발전은인간(2001년 2월 인간 게놈의 초안 발표)을 비롯한 생물체의 게놈구조가 규명되어 이 유전자구조정보를 web상에서 쉽게 알아낼 수 있는데서 비롯된다. 포스트게놈시대의 게놈기능연구를 총괄적으로 '기능유전체학 (Functional Genomics)'이라고하며 여기에는 핵산(DNA나 RNA)을 표적으로 게놈기능을 연구하는 genomics(유전체학, RNA발현을 대상으로 하는 transcriptomics(전사체학) 포함), 총체적인 단백체를 대상으로 유전자기능을 연구하는 proteomics(단백질체학) 및 대사물질을 대상으로 하는 metabolomics(대사체학), 이들 분야를 공통적으로 지원하는 bioinformatics(생물정보학)로 구분된다. 본 고에서는 프로테오믹스 분야를 중심으로 소개하고자 한다.

• Korean Journal of Food Science and Technology
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• v.8 no.1
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• pp.19-32
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• 1976

The laboratory Mejus as well as home-made Meju and improved Meju received from Korea were ripened in the brine for up to 8 months and the changes is the chemical composition during the process were determined and the differences between the types of Meju were compared. On the basis of the amino acid pattern, the changes in the protein quality of soybean during the process was evaluated. No significant changes in the general chemical composition of Meju were noticed during the ripening for 8 months. However, the nitrogen solubility of Meju increased for $13{\sim}29%$ to $66{\sim}78%$ during 8 month ripening of the Meju-brine mixture. The concentration of free amino-N to the total-N increased from $4{\sim}7%$ in Meju to $29{\sim}35%$ in the 8month ripened mixture. The concentration of amino-N to the total-N increased from $1{\sim}4%$ in Meju to $5{\sim}14%$ in the 8month ripened mixture and the changes varied with the type of Meju used. Remarkable changes in the amino acid pattern of soybean were occured during the ripening process. The concentration of methionine decreased to the half of original Meju during the first month of ripening. Arginine and histidine were destroyed rapidly by the ripening longer than 1 month. A considerable amount of ornithine was synthesized during the ripening. The amino acid pattern of Meju did change drastically during the ripening longer than 3 months and the changes varied with the type of Meju. The retention of the nutrients in soybean during 8 month ripening of the laboratory 3 month Meju in the brine was 49% for carbohydrates, 107% for crude fat, 93% for crude protein and 74% for the total amino acid. Histidine, arginine and methionine and 74% for the total amino acid. Histidine, arginine and methionine were the most damaged during the process, retaining only 25%, 27% and 49% of the contents in raw soybean, respectively, whereas lysine retained 79%. By the separation of the 8 month ripened mixture, approximately 60% of crude protein, all of crude fat and 80% of carbohydrates in the mixture were retained in soypaste. Soypaste contained higher concentrations of amino acids per 16gN compared to soysauce, except for lysine. The most limiting amino acid of the protein was the S-containing amino acids in all cases studied, whereas the second limiting amino acid varied from valine in soybean to threonine in most of Mejus and the brine mixtures, lysine in most of soypastes and tryptophan in some of soysauces. According to the protein quality evaluation made by the reference of the FAO provisional pattern of amino acid, the chemical score of raw soybean was 82, which was reduced to 77 by cooking and further reduced to $71{\sim}74$ by Meju fermentation. At the eighth month of ripening the chemical score of the Meju-brine mixtures were reduced to $51{\sim}66. After the separation, the chemical score of soypaste ranged from 60 to 71, whereas that of soysauce varied from 45 to 57. Generally, the products made from improved Meju recorded the highest score, whereas those made from homemade Meju showed the poorest protein quality. The essential amino acid index(EAAI) of the samples was similar to the chemical score, but it appeared to fit the overall changes in the amino acid pattern during the process better than the chemical score.

• Molecular & Cellular Toxicology
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• v.5 no.4
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• pp.323-327
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• 2009

• Monthly Duck's Village
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• s.57
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• pp.34-37
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• 2008

오리 농가의 수익에 가장 큰 영향을 미치는 것은 사료비이다. 균형이 잘 이루어진 사료는 오리의 생산성을 최대로 하고, 오리의 건강을 유지하는데 필수적이다. 오리의유지, 생산, 성장 그리고 번식을 위해서는 오리의 에너지/단백비를 충족하는 사료를 급여하여야 한다. 사료비를 낮게 유지하는것은 오리농가의 수입과 직결된다. 이를 위해서는 농장에서 직접 생산하는 양질의 조사료를 최대한 급여하고, 가능한 최소 비용으로 최적의 육용오리을 위한 사료를 급여관리하여야 할 것이다.

• Applied Biological Chemistry
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• v.35 no.4
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• pp.227-231
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• 1992

The plasmids pSUPBT and pSUPBTR were constructed with a vector pSUP2021 and the BT toxin gene in the plasmid pES 1. The plasmids constructed were introduced into the antagonistic rhizobacteria P. fluorescens KR164 by conjugation and P. fluorescens having pSUPBT and pSUPBTR were named P. fluorescens KR164(pSUPBT)#2, KR164(pSUPBT)#3, KR164(pSUPBTR)#2 and KR164(pSUPBTR)#3, respectively. The BT toxin gene were identified in all transformants by Southern hybridization and the final product of BT toxin gene was identified only in P. fluorescens KR164(pSUPBTR)#3 by SDS-PAGE. This crystal toxin protein were also observed in electron microscopy.

• The Journal of Natural Sciences
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• v.14 no.2
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• pp.55-65
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• 2004

A thiol-specific antioxidant(TSA) protein was purified from Earthworm, Lumbricus terrestris by DEAE-Cellulose, Phenl sepharose, Sephacryl S-200 gel filtration and HPLC S-300 Column Chromatography. This protein showed a thiol-specific antioxidant activity against inactivation of glutamine synthetase by a metal-catalysed oxidation system capable of generation reaction oxygen species. The molecular mass of the protein was determinated to be 51-kDa by SDS-polyacrylamide gel electrophores. Taken together, the purified TSA protein could be a new member of TSA family.

• Radiation Oncology Journal
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• v.17 no.2
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• pp.151-157
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• 1999

Purpose : By sequencing the Erpressed Sequence Tags of human 걸ermal papilla CDNA library, we identified a clone named K872 of which the expression decreased during differentiation of HL6O cell line. Materials and Methods : K872 plasmid DNA was isolated according to QIA plasmid extraction kit (Qiagen GmbH, Germany). The nucleotide sequencing was performed by Sanger's method with K872 plasmid DNA. The most updated GenBank EMBL necleic acid banks were searched through the internet by using BLAST (Basic Local Alignment Search Tools) program. Nothern bots were performed using RNA isolated from various human tissues and cancer cell lines. The gene expression of the fusion protein was achieved by His-Patch Thiofusicn expression system and the protein product was identified on SDS-PAGE. Results : K872 clone is 1006 nucleotides long, and has a coding region of 675 nucleotides and a 3' non-coding region of 280 nucleotides. The presumed open reading frame starting at the 5' terminus of K872 encodes 226 amino acids, including the initiation methionine residue. The amino acid sequence deduced from the open reading frame of K872 shares $70\%$, identity with that of rat glutathione 5-transferase kappa 1 (rGSTKl). The transcripts were expressed in a variety of human tissues and cancer cells. The levels of transcript were relatively high in those tissues such as heart, skeletal muscle, and peripheral blood leukocyte. It is noteworthy that K872 was found to be abundantly expressed in coloreetal cancer and melanoma cell lines. Conclusion : Homology search result suggests that K872 clone is the human homolog of the rGSTK1 which is known to be involved in the resistance of cytotoxic therapy. We propose that meticulous functional analysis should be followed to confirm that.