http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Ohmic heating시 Chemical marker를 이용한 입자식품의 살균도 평가
최양문,배송환,박장우 안성산업대학교 1997 論文集 Vol.29 No.1
Chemical market를 이용한 살균도의 평가는 B. stearothermophilus의 포자를 이용하여 행하였으며 chemical market의 전구체로는 10% glucose를 같은 소고기에 첨가하여 meatball를 만들었으며 사용한 ohmic heater는 용량이 5KW 연속적 살균장치를 사용하였다. 미생물의 사멸율과 chemical market의 생성율은 meatball의 중앙부위와 표면이 거의 비슷하거나 표면에서 오히려 높게 나타났다. 같은 온도에서 가열시 포자의 사멸율과 chemical market의 생성량과는 좋은 상관관계를 나타내었다. 따라서 chemical market는 입자식품 ohmic heating시 미생물학적 안정성을 평가하는데 사용될 것으로 사료된다. Microbial validation of the chemical marker approach was carried out using B spore beads and meatball contained 10% glucose. Experiments were performed with the 5 KW ohmic heating system. The rate for microbial destruction and chemical marker formation at the center of the meatball were either similar or higher than those at the surface. There existed a reasonably good correlation between decadic reduction of the spore and marker yield under different conditions as long as the temperature was same. These microbial validation of the chemical marker approach can be used to help obtain the safety of ohmic heating of particulate foods.
Mutant p53-Notch1 Signaling Axis Is Involved in Curcumin-Induced Apoptosis of Breast Cancer Cells
Bae, Yun-Hee,Ryu, Jong Hyo,Park, Hyun-Joo,Kim, Kwang Rok,Wee, Hee-Jun,Lee, Ok-Hee,Jang, Hye-Ock,Bae, Moon-Kyoung,Kim, Kyu-Won,Bae, Soo-Kyung The Korean Society of Pharmacology 2013 The Korean Journal of Physiology & Pharmacology Vol.17 No.4
Notch1 has been reported to be highly expressed in triple-negative and other subtypes of breast cancer. Mutant p53 (R280K) is overexpressed in MDA-MB-231 triple-negative human breast cancer cells. The present study aimed to determine whether the mutant p53 can be a potent transcriptional activator of the Notch1 in MDA-MB-231 cells, and explore the role of this mutant p53-Notch1 axis in curcumin-induced apoptosis. We found that curcumin treatment resulted in an induction of apoptosis in MDA-MB-231 cells, together with downregulation of Notch1 and its downstream target, Hes1. This reduction in Notch1 expression was determined to be due to the decreased activity of endogenous mutant p53. We confirmed the suppressive effect of curcumin on Notch1 transcription by performing a Notch1 promoter-driven reporter assay and identified a putative p53-binding site in the Notch1 promoter by EMSA and chromatin immunoprecipitation analysis. Overexpression of mutant p53 increased Notch1 promoter activity, whereas knockdown of mutant p53 by small interfering RNA suppressed Notch1 expression, leading to the induction of cellular apoptosis. Moreover, curcumin-induced apoptosis was further enhanced by the knockdown of Notch1 or mutant p53, but it was decreased by the overexpression of active Notch1. Taken together, our results demonstrate, for the first time, that Notch1 is a transcriptional target of mutant p53 in breast cancer cells and suggest that the targeting of mutant p53 and/or Notch1 may be combined with a chemotherapeutic strategy to improve the response of breast cancer cells to curcumin.
Optimization of Isoflavone Extraction from Soy Germ - Research Note-
Bae, Sang-Moon,Jang, Chan-Ho,Kim, Jang-Hoon,Lim, Hyun-Ae,Kim, Joo-Ryong,Kim, Jeong-Hwan,Kim, Jong-Sang The Korean Society of Food Science and Nutrition 2005 Preventive Nutrition and Food Science Vol.10 No.3
Soy isoflavones have drawn much attention due to their potential to prevent breast and prostate cancers, osteoporosis, heart disease, and other postmenopausal symptoms. Soy germ is one of the richest sources of isoflavones, and thus has good potential to be used as the ingredient of health foods. This study examined the extraction rate of isoflavones from soy germ at various conditions. After the effect of extraction temperature and duration on isoflavones extraction from soy germ was examined, the optimum concentration of ethanol as extraction solvent was determined. When ethanol concentration was fixed at $60\%\;(v/v)$, the maximum isoflavone extraction was achieved at 2 hrs and $30^{\circ}C$. Among various concentrations of ethanol tested, $80\%\;(v/v)$ ethanol showed the highest extraction efficiency. In conclusion, the maximum extraction of isoflavones was obtained using $80\%\;(v/v)$ ethanol as a solvent, at $30^{\circ}C$ of temperature, and 2 hrs of extraction time.
Optimization of Isoflavone Extraction from Soy Germ
Sang-Moon Bae,Chan Ho Jang,Jang-Hoon Kim,Hyun Ae Lim,Joo-Ryong Kim,Jeong Hwan Kim,Jong-Sang Kim 한국식품영양과학회 2005 Preventive Nutrition and Food Science Vol.10 No.3
Soy isoflavones have drawn much attention due to their potential to prevent breast and prostate cancers, osteoporosis, heart disease, and other postmenopausal symptoms. Soy germ is one of the richest sources of isoflavones, and thus has good potential to be used as the ingredient of health foods. This study examined the extraction rate of isoflavones from soy germ at various conditions. After the effect of extraction temperature and duration on isoflavone extraction from soy germ was examined, the optimum concentration of ethanol as extraction solvent was determined. When ethanol concentration was fixed at 60% (v/v), the maximum isoflavone extraction was achieved at 2 hrs and 30℃. Among various concentrations of ethanol tested, 80% (v/v) ethanol showed the highest extraction efficiency. In conclusion, the maximum extraction of isoflavones was obtained using 80% (v/v) ethanol as a solvent, at 30℃ of temperature, and 2 hrs of extraction time.
Mutant p53-Notch1 Signaling Axis Is Involved in Curcumin-Induced Apoptosis of Breast Cancer Cells
Yun-Hee Bae,Jong Hyo Ryu,Hyun-Joo Park,Kwang Rok Kim,Hee-Jun Wee,Ok-Hee Lee,Hye-Ock Jang,Moon-Kyoung Bae,Kyu-Won Kim,Soo-Kyung Bae 대한생리학회-대한약리학회 2013 The Korean Journal of Physiology & Pharmacology Vol.17 No.4
Notch1 has been reported to be highly expressed in triple-negative and other subtypes of breast cancer. Mutant p53 (R280K) is overexpressed in MDA-MB-231 triple-negative human breast cancer cells. The present study aimed to determine whether the mutant p53 can be a potent transcriptional activator of the Notch1 in MDA-MB-231 cells, and explore the role of this mutant p53-Notch1 axis in curcumin-induced apoptosis. We found that curcumin treatment resulted in an induction of apoptosis in MDA-MB-231 cells, together with downregulation of Notch1 and its downstream target, Hes1. This reduction in Notch1 expression was determined to be due to the decreased activity of endogenous mutant p53. We confirmed the suppressive effect of curcumin on Notch1 transcription by performing a Notch1 promoter-driven reporter assay and identified a putative p53-binding site in the Notch1 promoter by EMSA and chromatin immunoprecipitation analysis. Overexpression of mutant p53 increased Notch1 promoter activity, whereas knockdown of mutant p53 by small interfering RNA suppressed Notch1 expression, leading to the induction of cellular apoptosis. Moreover, curcumin-induced apoptosis was further enhanced by the knockdown of Notch1 or mutant p53, but it was decreased by the overexpression of active Notch1. Taken together, our results demonstrate, for the first time, that Notch1 is a transcriptional target of mutant p53 in breast cancer cells and suggest that the targeting of mutant p53 and/or Notch1 may be combined with a chemotherapeutic strategy to improve the response of breast cancer cells to curcumin.
Moon, Jeong-Chan,Hah, Young-Sool,Kim, Woe-Yeon,Jung, Bae-Gyo,Jang, Ho-Hee,Lee, Jung-Ro,Kim, Sun-Young,Lee, Young-Mee,Jeon, Min-Gyu,Kim, Choong-Won,Cho, Moo-Je;,Lee, Sang-Yeol Plant molecular biology and biotechnology research 2005 Plant molecular biology and biotechnology research Vol.2005 No.
Although biochemical properties of 2-Cys peroxiredoxins (Prxs) have been extensively studied, their real physiological functions in higher eukaryotic cells remain obscure and certainly warrant further study. Here we demonstrated that human (h) PrxⅡ, a cytosolic isotype of human 2-Cys Prx, has dual functions as a peroxidase and a molecular chaperone, and that these different functions are closely associated with its adoption of distinct protein structures. Upon exposure to oxidative stress, hPrxⅡ assumes a high molecular weight complex structure that has a highly efficient chaperone function. However, the subsequent removal of stressors induces the dissociation of this protein structure into low molecular weight proteins and triggers a chaperone-to-peroxidase functional switch. The formation of a high molecular weight hPrxⅡ complex depends on the hyperoxidation of its N-terminal peroxidatic Cys residue as well as on its C-terminal domain, which contains a "YF motif" that is exclusively found in eukaryotic 2-Cys Prxs. A C-terminally truncated hPrxⅡ exists as low and oligomeric protein species and does not respond to oxidative stress. Moreover, this C-terminal deletion of hPrxⅡ converted it from an oxidation-sensitive to a hyperoxidation-resistant form of peroxidase. When functioning as a chaperone, hPrxⅡ protects HeLa cells from H_(2)O_(2)-induced cell death, as measured by a terminal deoxynucleotidyltransferase-mediated dUTP nickend labeling assay and fluorescence-activated cell sorting analysis.