• Journal of the Korean Society of Food Science and Nutrition
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• v.25 no.5
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• pp.831-838
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• 1996

This study was undertaken in order to elucidate the effects of raw, roast and steamed buckwheat on fecal protein, Pancreas weight, the activities of $\alpha-amylase,$ chymotrypsin and lipase 91 the pancreas, and $\alpha-amylase,$ chymotrypsin and trypsin activities of the feces in streptozotocin-induced diabetic rats. Fecal proteins of raw, roast and steamed buckwheat diabetic groups were increased up to 99%, 91%, 103%, respectively compared to those of the diabetic control group. Feeding of buckwheat diet increased pancreas weight, especially raw buckwheat diabetic group(p<0.05). Pancreatic chymo-trypsin activity was decreased in buckwheat diabetic groups compared to diabetic control group, wheres any significant difference was observed in $\alpha-amylase$ and lipase activities. Fecal chymotrypsin activi-ty was significantly increased in all buckwheat diabetic groups. Fecal trypsin activity was increased in roast buckwheat diabetic groups compared to diabetic control group and fecal $\alpha-amylase$ activity in buckwheat diabetic group was not significantly different. These results suggest that feeding of buckwheat diet enhances the impaired exocrine pancreatic function of diabetic rat.

• Journal of Microbiology and Biotechnology
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• v.28 no.12
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• pp.2079-2094
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• 2018

Sunflower trypsin inhibitor (SFTI) is a 14-amino-acid bicyclic peptide that contains a single internal disulfide bond. We initially constructed chimeras of SFTI with N-terminal secretion signals from the Escherichia coli OmpA and Pseudomonas aeruginosa ToxA, but only detected small amounts of protease inhibition resulting from these constructs. A substantially higher degree of protease inhibition was detected from a C-terminal SFTI fusion with E. coli YebF, which radiated more than a centimeter from an individual colony of E. coli using a culture-based inhibitor assay. Inhibitory activity was further improved in YebF-SFTI fusions by the addition of a trypsin cleavage signal immediately upstream of SFTI, and resulted in production of a 14-amino-acid, disulfide-bonded SFTI free in the culture supernatant. To assess the potential of the secreted SFTI to protect the ability of a cytotoxic protein to kill tumor cells, we utilized a tumor-selective form of the Pseudomonas ToxA (OTG-PE38K) alone and expressed as a polycistronic construct with YebF-SFTI in the tumor-targeted Salmonella VNP20009. When we assessed the ability of toxin-containing culture supernatants to kill MDA-MB-468 breast cancer cells, the untreated OTG-PE38K was able to eliminate all detectable tumor cells, while pretreatment with trypsin resulted in the complete loss of anticancer cytotoxicity. However, when OTG-PE38K was co-expressed with YebF-SFTI, cytotoxicity was completely retained in the presence of trypsin. These data demonstrate SFTI chimeras are secreted in a functional form and that co-expression of protease inhibitors with therapeutic proteins by tumor-targeted bacteria has the potential to enhance the activity of therapeutic proteins by suppressing their degradation within a proteolytic environment.

• Investigative Magnetic Resonance Imaging
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• v.8 no.2
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• pp.100-108
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• 2004

Purpose : Early degeneration of articular cartilage is accompanied by a loss of glycosaminoglycan (GAG) and the consequent change of the integrity. The purpose of this study was to biochemically quantify the loss of GAG, and to evaluate the $Gd(DTPA)^{2-}$-enhanced, and T1, T2, rho relaxation map for detection of the early degeneration of cartilage. Materials and Methods : A cartilage-bone block in size of $8mm\;\times\;10mm$ was acquired from the patella in each of three pigs. Quantitative analysis of GAG of cartilage was performed at spectrophotometry by use of dimethylmethylene blue. Each of cartilage blocks was cultured in one of three different media: two different culture media (0.2 mg/ml trypsin solution, 1mM Gd $(DTPA)^{2-}$ mixed trypsin solution) and the control media (phosphate buffered saline (PBS)). The cartilage blocks were cultured for 5 hrs, during which MR images of the blocks were obtained at one hour interval (0 hr, 1 hr, 2 hr, 3 hr, 4 hr, 5 hr). And then, additional culture was done for 24 hrs and 48 hrs. Both T1-weighted image (TR/TE, 450/22 ms), and mixed-echo sequence (TR/TE, 760/21-168ms; 8 echoes) were obtained at all times using field of view 50 mm, slice thickness 2 mm, and matrix $256\times512$. The MRI data were analyzed with pixel-by-pixel comparisons. The cultured cartilage-bone blocks were microscopically observed using hematoxylin & eosin, toluidine blue, alcian blue, and trichrome stains. Results : At quantitation analysis, GAG concentration in the culture solutions was proportional to the culture durations. The T1-signal of the cartilage-bone block cultured in the $Gd(DTPA)^{2-}$ mixed solution was significantly higher ($42\%$ in average, p<0.05) than that of the cartilage-bone block cultured in the trypsin solution alone. The T1, T2, rho relaxation times of cultured tissue were not significantly correlated with culture duration (p>0.05). However the focal increase in T1 relaxation time at superficial and transitional layers of cartilage was seen in $Gd(DTPA)^{2-}$ mixed culture. Toluidine blue and alcian blue stains revealed multiple defects in whole thickness of the cartilage cultured in trypsin media. Conclusion : The quantitative analysis showed gradual loss of GAG proportional to the culture duration. Microimagings of cartilage with $Gd(DTPA)^{2-}$-enhancement, relaxation maps were available by pixel size of $97.9\times195\;{\mu}m$. Loss of GAG over time better demonstrated with $Gd(DTPA)^{2-}$-enhanced images than with T1, T2, rho relaxation maps. Therefore $Gd(DTPA)^{2-}$-enhanced T1-weighted image is superior for detection of early degeneration of cartilage.

• Biomolecules & Therapeutics
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• v.5 no.3
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• pp.223-227
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• 1997

The protective effect of human urinary trypsin inhibitor(UTI) on acute hemorrhagic shock in beagle dog was studied. Hemorrhagic shock was experimentally induced in thoracotomized beagle dogs by removing blood and maintaining low arterial blood pressure for 30 min, and then blood removed was entirely transfused back into the dogs within one hour. When the blood was transfused, UTI was administered together to check the potential protective effect of UTI on hemorrhagic shock. The arterial blood pressure recovery was accelerated slightly by UTI treatment. Blood pH and $P_{a co2}$ returned to normal level in shorter time in the UTI treatment group. These data suggest that UTI may have protective effects on experimentally induced hemorrhagic shock.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1996.04a
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• pp.165-165
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• 1996

균의 감염에 의해 유도되는 패혈성 shock는 균이 분비하는 elastase가 관여하며, 외부에서 serine pretense inhibitor의 biopolymer의 투여로 균에 의해 유도된 패혈성 shock를 억제시킬 수 있다고 보고되고 있다. 이에 본 연구진은 패혈성 치료제의 개발의 목적으로, 국내에서 민간 약으로 많이 이용되고 있는 백편두로부터 새로운 elastase inhibitor를 분리, 정제하여 부분 아미노산 서열 및 특성을 조사하였기에 발표하고자 한다. 백편두 추출액을 여러 차례에 걸쳐 column chromatography을 수행하면서 얻어지는 각 fraction에 대하여 elastase MCA-기질 및 trypsin MCA-기질을 이용하여 활성 측정 후 elastase 기질 및 trypsin 기질에 대하여 활성을 억제하는 fraction들을 모아 $C_{18}$ open column chromatography 및 $C_{18}$ HPLC 과정을 수행하여 2종류의 trypsin 활성 억제 물질과 1종류의 elastase inhibitor를 분리, 정제하여 각각을 Ti1, Ti2 및 Ti3로 명명하였다. 전기영 동 상에서 단일 hand를 확인한 후 각각의 inhibitor들의 부분 아미노산 서열을 결정하였다.

• Journal of Nutrition and Health
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• v.4 no.4
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• pp.25-28
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• 1971

The effects of additives for food and drug upon the tryptic hydrolysis of casein an a Synthetic substrate, $N^{\alpha}-Benzoyl-L-arginine$ ethylester (BAEE) in vitro has been studied. The results of this study were summarized as follows 1) It was found that the action of inhibition became stronger in the following order: Methyl parabene>Rose Bengal> Phloxine> Sod. DHA> Erythrosine by the colorimetric method using BAEE. These results also showed that other additives had no effect on the activity of trypsin. 2) All samples tested showed respectively same tendency using casein in this method. But the activity by Erythrosine and Sod. DHA was slightly increased in this experiment.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.1
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• pp.68-72
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• 1993

The methanol extract of the leaves of Cudrania tricuspidata and ethyl acetate fraction from the methanol extract showed inhibition for trypsin activity and the growth inhibition of Staphylococcus aureus. The content of kaempferol 7-O-$\beta$-D-glucopyranoside isolated from this plant was determined by HPLC and it was about 0.31% for the methanol extract.

• Journal of Pharmaceutical Investigation
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• v.5 no.4
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• pp.24-31
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• 1975

This paper attempts to investigate the effect of proteolytic enzyme on the absorption and excretion of pyrazinamide. The rat small intestinal absorption of pyrazinamide in the presence of proteolytic enzyme such as chymotrypsin and compounding enzyme (chymotrypsin and trypsin) are increasingly absorbed, but in the trypsin are similar to that of control. Blood levels of pyrazinamide after rabbit's duodenum injection are significantly enhenced to correspond to 112-120% by proteolytic enzymes concentration respectively, but both on the high concentration of chymotrypsin and the low concentration of trypsin are insignificantly enhenced. Proteolytic enzymes do not give the effect on clearance of pyrazinamide. Proteolytic enzymes give the effect on absorption of pyrazinamide, but do not give the effect on excretion of pyrazinamide.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2006.05a
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• pp.269-271
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• 2006

Casein과 whey의 가수분해 물에 대한 항산화 능을 측정하기 위해 연구를 수행하였다. pH에 따른 Total antioxidant capacity(TAC)는 casein 및 whey 모두 pH 6.0 에서 보다 pH 7.4에서 더 높은 TAC 결과를 나타내었다. Casein이 whey보다 농도가 증가함에 따라 TAC 값이 증가하였으며 이는 배양시간이나 pH에 따른 TAC 측정에서와 같이 casein이 whey보다 더 높은 TAC 값을 나타내고 있으나, $2,000{\mu}g/mL$에서는 TAC 값이 감소하여 casein, whey 모두 유사한 TAC 값을 나타내었다. Trypsin에 의한 casein 및 whey의 가수분해는 반응 10분 이후부터는 NPN 량이 더 이상 증가하지 않았으며 casein보다 whey가 분해율이 낮았다. Trypsin처리한 casein과 whey의 TAC를 측정한 결과로서 trypsin 처리구가 무처리구에 비해 높은 TAC 결과를 나타내었다.

• Journal of Pharmaceutical Investigation
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• v.4 no.1_2
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• pp.31-38
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• 1974

The effort of proteolytic enzyme on the absorption and excretion of sulfadimethoxine are investigated in this paper. The rat small intestinal absortion of sulfadimethoxine in the presence of proteolytic enzymes such as chymotrypsin and trypsin are increasingly absorbed more than 20% during 3 hours. Blood levels of sulfadimethoxine following oral administration are not effected by proteolytic enzyme, but both on the high concentration of chymotrypsin and the low concentration of trypsin at only 3 and 4 hours are increased(P<0.05) from that of the control . Blood levels of sulfadimethoxine after duodenum injection are remakably enhensed to correspand to 18.5-25.0% (P<0.01) by the proteolytic enzyme concentration respectively. Proteolytic enzymes did not give influence on excretions of sulfadimethoxine after duodenum and oral administration.