• Korean journal of food and cookery science
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• v.24 no.3
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• pp.304-311
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• 2008

This study examined Jeung-pyun(JP) Retrogradation in samples containing 3% whole protein, 7S protein, or 11S protein(w/w) that were stored at $4^{\circ}C$ for 6, 12, 24 and 72 hr. Rheometery and differential scanning calorimetry(DSC) were used in the analysis. The pH of the dough decreased during the fermentation process, but it increased after steaming. The JP prepared with soybean protein isolate(SPI) had higher pH than the control group. During storage the textural characteristics of the JP showed effects according to the additions of SPI. After 6 hr of storage, the JP samples containing soybean flour, whole protein, 7S protein, and 11S protein had lower hardness valuse. From 4 hr to 12 hr, higher springiness values were found in the samples containing whole protein, 7S protein and 11S protein. At 0 hr, the control group had the highest cohesiveness value, but after 24 hr it presented the lowest value. For gumminess, after 6 hr of storage, the control group offered the lowest value. Whereas after 12 hr of storage the whole protein group showed the highest value, and at 24 hr, the whole protein, 7S protein, and 11S protein groups had higher values. According to the DSC results, the 11S protein group had lower enthalpy values(${\bigtriangleup}H$) suggesting that adding 11S protein to JP might improve starch retrogradation. After 72 hr of storage, the control group had the highest onset temperature($T_{o}$) and peak temperature($T_{p}$) whereas the 7S and 11S protein JP samples had higher conclusion temperatures($T_{c}$). Therefore, based on the different analysis result between the control and treatment groups, the addition of SPI to Jp had effects on retrogradation.

• Journal of Cancer Prevention
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• v.23 no.4
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• pp.153-161
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• 2018

Imbalance of protein homeostasis (proteostasis) is known to cause cellular malfunction, cell death, and diseases. Elaborate regulation of protein synthesis and degradation is one of the important processes in maintaining normal cellular functions. Protein degradation pathways in eukaryotes are largely divided into proteasome-mediated degradation and lysosome-mediated degradation. Proteasome is a multisubunit complex that selectively degrades 80% to 90% of cellular proteins. Proteasome-mediated degradation can be divided into 26S proteasome (20S proteasome + 19S regulatory particle) and free 20S proteasome degradation. In 1980, it was discovered that during ubiquitination process, wherein ubiquitin binds to a substrate protein in an ATP-dependent manner, ubiquitin acts as a degrading signal to degrade the substrate protein via proteasome. Conversely, 20S proteasome degrades the substrate protein without using ATP or ubiquitin because it recognizes the oxidized and structurally modified hydrophobic patch of the substrate protein. To date, most studies have focused on protein degradation via 26S proteasome. This review describes the 26S/20S proteasomal pathway of protein degradation and discusses the potential of proteasome as therapeutic targets for cancer treatment as well as against diseases caused by abnormalities in the proteolytic system.

• Journal of Yeungnam Medical Science
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• v.31 no.1
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• pp.52-55
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• 2014

Protein S deficiency is one of the several risk factors for thrombophilia and can cause blood clotting disorders such as deep vein thrombosis and pulmonary embolism. A 54-year-old man was admitted with the complaint of dyspnea and was diagnosed with pulmonary embolism. The patient had very low level of free protein S, total protein S antigen, and protein S activity (type I protein S deficiency). In history taking, we found that his mother, 78 year old, had a history of same disease 10 years ago, and confirmed the pronounced low level of protein S. The patient's son also had very low level of protein S, however there had not been any history of pulmonary embolism yet. This case study suggests that asymptomatic persons with a family history of protein S deficiency and pulmonary embolism should be checked regularly for early detection of the disease, as protein S deficiency can be suspected.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.33 no.s01
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• pp.39-47
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• 1988

Soybean grain is most widely used and soybean crop produces most high protein per area among crops. To meet rapid increase of human population and supply protein in safety. soybean has considered more and more important crop. And it has been emphasizing that high quality and high protein soybean breeding must be made efforts in future. Many papers related to soybean breeding for high quality and protein and soybean protein composition have suggested the problems to do in future. Soybean germplasm collection. classification and conservation should be continuously performed, and it is emphasized that wild type of soybeans (G. soja) be considered to use in breeding for high protein varieties. Selections would be better emphasized in first yield and therefore high yield of protein per area. Selection for high protein would be secondary criterion. High protein lines with high yielding potential could be selection from certain populations, and breeders should consider this phenomenon in procedure of selection. Heritability of protein percent is relatively high and genetic gain of increment of protein percent is large. Soybean protein which is comprised 70 to 90% of globulin is constituted mostly 11S and 7S proteins. Sulfur-containing amino acids, methionine and cysteine, are identified to contain more in 11S protein than 7S protein. High 11S germplasm should be desirable to use in crossing plan, and selection of high ratio of 11S/7S lines be better in development of high quality varieties.

• Journal of Nutrition and Health
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• v.29 no.6
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• pp.578-589
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• 1996

This study was performed to invstigate the effect of dietary protein level and source on cadmium intoxicification in rats. Forty-eight male rats of Sprague-Dawley strain weighing 171$\pm$3g were blocked into 8 groups of 6 animals according to body weigth, and were raised for 30days. Eight experimental diets different with cadmium(0ppm, 400ppm)and protein(15%, 40%) levels and protein source[casien, I.S.P.(isolated soy protein)] were given to animals for 30days. Food intake, weight gain, food efficiency ratio, liver weight, kidney weight and femur weight were lower in cadmium added group, and higher in high protein groups(40% protein) than medium protein groups(15% protein). But, dietary protein source had no influence on them. Cadmium concerntration of liver was higher in rats fed casein than I.S.P. groups, and cadmium concentration in intestine was higher in high protein groups. In femur both high protein and I.S.P.diets increased cadmium concentrations. MT concdentrations in liver, kidney and intestine were higher in cadmium added group, and kidney intestine MT concentration were higher in high protein group. Absorption and retention rates of cadmium were lower in rat fed I.S.P. than animal fed casein among medium protein groups and cadmium concentration in blood and liver of I.S.P groups were lower than casein groups. But absorption and retention rates of cadmium were similar in high casein and I.S.P. groups. Renal damage by cadmium administration was not seen in all groups. Absorption rates of zinc and copper competing with cadmium in absorption process were lower in high protein groups than medium protein groups and lower in rats fed I.S.P. than casein. In conclusion, weight gain, F.E.R, and MT concentraion of high protein groups were higher than those of medium protein groups and absorption and retention rates of cadmium were lower in high protein groups. From these results, it was shown that cadmium toxicity was alleviated by high dietary protein. Meanwhile, the effect of dietary source on the cadmium toxicity was different with protein level. In medium protein groups absorption and retention rates of cadmium were much lower in rats fed I.S.P. than casein. In high protein groups, cadmium toxicity was not influenced by protein source and absorption and retention rates of cadmium were not different between casein and I.S.P. groups.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.44 no.4
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• pp.350-354
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• 1999

Soybean varieties derived from Korea are classified into four groups on the basis of their food types such as soybeans for vegetable, sprout, sauce and paste and soybeans with colored seed coat. This study was carried out to know the differences in storage protein concentrations among these four groups. There were differences in storage protein concentrations among four groups. In 7S protein, the $\alpha$'-and $\alpha$-subunit concentrations did not vary among four groups, while a $\beta$-subunit concentration greatly varied. 7S protein concentration was the highest(40.6%) in soybean for sauce and paste and the lowest(37.7%) in soybean for vegetable, while 11S protein concentration was the highest (62.3%) in soybean for vegetable and the lowest (59.4%) in soybean for sauce and paste. In view of the fact that 11S protein has much higher sulfur containing amino acids than 7S protein, it was shown the soybeans for vegetable may have higher nutrition value than other groups.

• Korean Journal of Head & Neck Oncology
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• v.9 no.1
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• pp.74-87
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• 1993

Immunohistochemical studies on S-100 protein and lactoferrin were carried out to evaluate the existence and distribution pattern of S-100 protein and lactoferrin positive cells in salivary gland tumors. The specimens used were 25 cases of pleomorphic adenoma, 2 cases of monomorphic adenoma, 2 cases of mucoepidermoid tumor, 2 cases of acinic cell tumor, 3 cases of adenoid cystic carcinoma and 2 cases of adenocarcinoma occured in parotid and submandibular salivary gland. ABC kits(Dako corp. Copenhagen. Denmark) for S-100 protein and lactoferrin were used. The results obtained were summarized as follows: In the normal salivary gland. positive immunoreaction for S-100 protein was observed in myoepithelial cells of acini and intercalated ducts. Positive immunoreaction for lactoferrin was observed in serous acinic cells, epithelial cells of intercalated ducts, and excretory material in the ductal lumina. In the pleomorphic and monomorphic adenomas. most of tumor cells were positive for S-100 protein, while luminal tumor cells in gland-like or duct-like structures were rarely positive for lactoferrin. In mucoepidermoid tumor, most of squamous cells and a few of intermediate cells were positive for S-100 protein, but all of tumor cells were negative for lactoferrin. In acinic cell tumor, most of tumor cells were positive for lactoferrin, but all of tumor cells were negative for S-100 protein. In adenoid cystic carcinoma, basaloid tumor cells in trabecular structure were focally positive for S-100 protein. and in adenocarcinoma, many of tumor cells were posivive for both S-100 protein and lactoferrin. Thus, according to the embryonic stage of the development of the tumor cell origin, it was possible to classify the salivary gland tumor as followings: mucoepidermoid carcinoma which originated from the earliest stage, acinic cell tumor which originated from the end stage. Between these two extremes, there were pleomorphic adenoma, adenoid cystic carcinoma and adenocarcinoma which originated in the middle stage of the development of .the salivary glands. Based on the above results, it can be stated that S-100 protein is demonstrated in tumor cells orginated from myoepithelial cells and lactoferrin in glandular differentiated tumor cells.

• Journal of Microbiology
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• v.37 no.2
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• pp.86-89
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• 1999

An OTHBVS cell line from HepG2 was established. This cell line stably expresses the human hepatitis B virus (HBV) middle S protein that includes the preS2 region which is important for HBV particle entry into the hepatocyte. To establish this cell line, the middle S open reading frame (ORF), with a promoter located in the 5' region and enhancer located in the 3' region, was cloned downstream from the metallothionine (MT) promoter of the OT1529 vector. In this vector, expression of the middle S protein was constructed to be regulated by its own promoter and enhancer. Expression of the large S protein which contains the preS1 region in addition to the middle S protein was designed to be regulated by the MT promoter. When extracts of OTHBVS cells were examined with an S protein detection kit (RPHA, Korea Green Cross Co.), an S protein was detected. Total mRNA of OTHBVS cell examined by northern blot analysis with an S ORF probe revealed small/middle S transcripts (2.1 kb). When the MT promoter was induced by Zn, large S transcripts (2.4 kb) were detected. The GP36 and GP33 middle S proteins were presumably detected, but large S proteins were not detected by immunostain analysis using anti-preS2 antibody.

• The Microorganisms and Industry
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• v.19 no.4
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• pp.32-35
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• 1993

ras는 활성화 형태인 GTP bound form과 비활성화 형태인 GDP bound form의 두 형태로 존재하며 두 형태를 매개하는 regulatory protein들에 의해 그 activity가 조절된다. 또한 ras는 GTP와 GDP에 강한 친화성이 있으며 세포내에는 GTP보다 GDP가 더 많이 있어서 평소에는 ras가 GDP와 결합하고 있다가 활성화될때만 GTP와 결합하는 것으로 추정된다. GDP bound ras는 guanine nucloetide exchange protein(GEP)에 의해 활성화된 GTP bound form으로 전환되며 ras의 기능이 발휘된 후에는 GTPase activating protein(GAP)에 의해 비활성화된다. Yeast의 경우 IRA1과 2의 product가 GAP의 역할을 하는 것으로 알려져 있고 CDC25 gene의 product가 GEP의 기능을 담당하는 것으로 알려져 있다. NF1 gene은 Von Recklinghausen Neurofibromatosis Type I 질병을 가진 환자에게서 발견되었는데 부분적으로 sequencing한 결과에 따르면 yeast의 IRA1/2, mammalian GAP gene product와 protein homology가 높은 것으로 나타났다. Yeast의 경우 IRA1/2 gene의 손실이나 mammalian ras gene의 transformation으로 인한 heat shock sensitivity가 NF1 gene(2,3) 혹은 GAP(4)의 expression으로 suppression된 것으로 보아 NF1이 GAP protein으로서 ras를 불활성화 시킨다는 것이 판명되었다. 결론적으로 ras의 활성은 GTP bound 혹은 GDP bound의 양쪽형태를 이동하면서 조절되는데 이 기능은 GAP과 GEP 또는 그의 유사 protein들에 의해 수행되며 이러한 regulatory protein들은 growth factor, cytokine 그리고 protein kinase 같은 signal에 의해 활성화된다고 생각된다. 본 총설에서는 ras protein의 여러가지 성질보다는 ras의 modification과 관련하여 항암제로 사용할 수 있는 ras에 specific한 약품개발의 가능성과 현재 알려진 ras의 inhibitor를 중심으로 논하고자 한다.

• Asian-Australasian Journal of Animal Sciences
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• v.26 no.11
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• pp.1644-1650
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• 2013

Ribosomal protein (rp) S6 is the substrate of ribosomal protein S6K (S6 kinase) and is involved in protein synthesis by mTOR/S6K/S6 signaling pathway. Some S6 cDNA have been cloned in mammals in recent years but has not been identified in the goat. To facilitate such studies, we cloned the cDNA encoding Cashmere goat (Capra hircus) S6 (GenBank accession GU131122) and then detected mRNA expression in seven tissues by real time PCR and protein expression in testis tissue by immunohistochemisty. Sequence analysis indicated that the obtained goat S6 was a 808 bp product, including a 3' untranslated region of 58 bp and an open reading frame of 750 bp which predicted a protein of 249 amino acids. The predicted amino acid sequence was highly homologous to cattle, human, mouse and rat S6. Expression analysis indicated S6 mRNA was expressed extensively in detected tissues and S6 protein was expressed in testis tissue.