• Journal of Animal Environmental Science
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• v.10 no.2
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• pp.119-126
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• 2004

The protein in the extracts from the skins of pineapple and kiwi and the optimal conditions to hydrolyze blood, egg and gluten meals with them were investigated. Protein analysis by SDS-polyacylamide gel electrophoresis showed one protein band with 22 kd molecular weight in the pineapple skin extract, and Hve protein bands with 27 kd, 22.5 kd, 22 kd, 19 kd, and 14.4 kd molecular weight in the kiwi skin extract. The 22 kd protein in the pineapple skin extract is assumed to be bromelain, and the 27 kd protein in the kiwi skin extract is assumed to be actinidin, both are pretense. The optimal conditions for hydrolysis of blood, egg, and gluten meals we: 6-24 hours in time, $60^{\circ}C$ in temperature, and pH 4-pH 7.

• KSBB Journal
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• v.11 no.4
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• pp.438-444
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• 1996

Using recombinant Vaccinia virus(vSC8) that express ${\beta}$-galactosidase, a model heterologous protein, conditions for virus and protein production were investigated in tissue culture flask. As host animal cells HeLa and HeLa S3 were used. It was demonstrated that cells infected during the exponential growth phase gave higher protein yield than those infected during the stationary growth phase and calf serum concentration after virus infection did not significantly alter protein yield. Pretreatment of cell layer with hypotonic solution enhanced the virus infectivity. Optimum cell growth and recombinant protein production was achieved at $37^{\circ}C$. But, during 2 hours of virus infection period incubation temperature must be lowered to 20∼$30^{\circ}C$ for maximum recombinant protein yield. To enhance virus replication, the effects of adrenal glucocorticoid hormone (Dexamethasone) and silkworm hemolymph were evaluated. Only dexamethasone increased about 20% of ${\beta}$-galactosidase yield in HeLa S3 cells when added with 10-7∼10-5M concentration 24 hours before infection.

• Asian Pacific Journal of Cancer Prevention
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• v.15 no.22
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• pp.9853-9857
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• 2014

Background: The morbidity and mortality rate of liver cancer continues to rise in China and advanced cases respond poorly to chemotherapy. Ribosomal protein L24 has been reported to be a potential therapeutic target whose depletion or acetylation inhibits polysome assembly and cell growth of cancer. Materials and Methods: Total RNA of cultured amycin-resistant and susceptible HepG2 cells was isolated, and real time quantitative RT-PCR were used to indicate differences between amycin-resistant and susceptible strains of HepG2 cells. Viability assays were used to determine amycin resistance in RPL24 transfected and control vector and null-transfected HepG2 cell lines. Results: The ribosomal protein L24 transcription level was 7.7 times higher in the drug-resistant HepG2 cells as compared to susceptible cells on quantitative RT-PCR analysis. This was associated with enhanced drug resistance as determined by methyl tritiated thymidine (3H-TdR) incorporation. Conclusions: The ribosomal protein L24 gene may have effects on drug resistance mechanisms in hepatocellular carcinoma HepG2 cells.

• Asian Pacific Journal of Cancer Prevention
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• v.13 no.5
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• pp.1823-1827
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• 2012

The gene encoding the Nin one binding (NOB1) protein which plays an essential role in protein degradation has been investigated for possible tumor promoting functions. The present study was focused on NOB1 as a possible therapeutic target for breast cancer treatment. Lentivirus mediated NOB1 siRNA transfection was used to silence the NOB1 gene in two established breast cancer cell lines, MCF-7 and MDA-MB-231, successful transfection being confirmed by fluorescence imaging. NOB1 deletion caused significant decline in cell proliferation was observed in both cell lines as investigated by MTT assay. Furthermore the number and size of the colonies formed were also significantly reduced in the absence of NOB1. Moreover NOB1 gene knockdown arrested the cell cycle and inhibited cell cycle related protein expression. Collectively these results indicate that NOB1 plays an essential role in breast cancer cell proliferation and its gene expression could be a therapeutic target.

• Asian-Australasian Journal of Animal Sciences
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• v.16 no.9
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• pp.1285-1290
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• 2003

The present study was carried out to investigate the effect of test day milk yield, test day evening milk yield, parity, stage of lactation and body weight on milk urea and milk protein concentration. A total of 319 milk samples was collected from buffaloes over four month's period and subjected to urea and protein analysis. Milk urea concentration (mg/dl) was significantly (p<0.01) increased with increasing test day milk yield. The lowest value ($57.03{\pm}1.13$) was observed in the milk yield group ${\leq}4.5kg/day$ and the highest value ($64.15{\pm}1.13$) in the group 7.7-10.7 kg/day. However, test day evening milk yield had no significant effect on milk urea concentration. Milk protein did not vary significantly with the test day milk yield as well as test day evening milk yield. A clear decreasing trend of milk urea concentration (mg/dl) was found with the increasing parity. The highest MU concentration ($64.03{\pm}1.14$) was found in the first parity and the lowest ($55.67{\pm}1.22$) was found in the sixth and above parity. Whereas, stage of lactation had no effect on milk urea concentration. Moreover, parity and stage of lactation did not have any significant effect on milk protein concentration. Body weight (kg) was also found negatively (p<0.05) related with urea content (mg/dl) in milk. The highest mean MU concentration ($64.34{\pm}0.88$) was found when body weight was between 532 and 598 kg and lower mean values ($59.24{\pm}0.94$ and $59.33{\pm}1.23$) were observed in 599 to 665 kg and ${\geq}666kg$ group. Body weight also had significant (p<0.05) effect on milk protein content. The highest milk protein content (%) was found in ${\geq}666kg$ group and the lowest in <531 kg group. In conclusion, for proper interpretation of milk urea values to monitor protein nutrition status of the buffaloes parity, milk yield and body weight should be considered.

• Asian Pacific Journal of Cancer Prevention
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• v.16 no.7
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• pp.2883-2887
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• 2015

Background: The calcium-binding S100A4 protein is involved in epithelial to mesenchymal transition, oncogenic transformation, angiogenesis, cytoskeletal integrity, mobility and metastasis of cancer cells. This study aimed to clarify the roles of S100A4 in genesis and progression of glioma. Materials and Methods: S100A4 expression was examined by real-time RT-CPR and Western blot in glioma and paired normal brain tissue (n=69), and compared with clinicopathological parameters of tumors. In addition, glioma U251 cells transfected with an S100A4-expressing plasmid were examined for proliferation by MTT, apoptosis by Annexin V-FITC, and migration and invasion with Transwell chambers. Results: Increased S100A4 mRNA expression was found in gliomas, compared with paired non-tumor tissue (p<0.001). Gradual elevation of overexpression of S100A4 was observed with increasing glioma grade (p<0.001). Astrocytoma showed lower S100A4 mRNA expression than oligodendrogliomas, with glioblastomas having highest values (p<0.001). Similar results were obtained for S100A4 protein, a positive link being found between mRNA and protein expression in gliomas (p<0.001). There was higher growth, lower apoptosis, stronger migration and invasion of S100A4 transfectants than control and mock transfected cells (p<0.001). Conclusions: These findings indicate that up-regulated S100A4 expression is positively linked to pathogenesis, progression and histogenesis of glioma by modulating proliferation, apoptosis, migration and invasion.

• Journal of Life Science
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• v.28 no.4
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• pp.478-482
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• 2018

Human rotavirus is a causative agent of acute diarrhea among children. The artificial gene encoding the truncated $VP8^*$ protein of human rotavirus A (serotype 1 strain WA) was synthesized according to the Escherichia coli codon preference. The synthetic $VP8^*$ gene also possessed the NdeI and HindIII restriction sites for the convenient in-frame cloning for translation and a 6-histidine tag at C-terminus for Ni+ affinity purification. Molecular weight of the truncated $VP8^*$ protein deduced from the nucleotide sequences of the artificial gene was a 19.7-kDa. This synthetic $VP8^*$ DNA fragment was inserted into the pT7-7 expression vector and transformed into E. coli BL21 (DE3). Transformants harboring the synthetic gene encoding the $VP8^*$ protein was induced by supplement of a final concentration of 0.05 mM ITPG at $20^{\circ}C$. Protein crude extract from the E. coli transformants was subjected to Western blotting with the mouse anti-rotavirus capsid antibody, showing ~20-kDa $VP8^*$ protein band. The truncated $VP8^*$ protein band was also observed by Western blotting using the rabbit polyclonal antibody serum made against the truncated $VP8^*$ protein. This study suggested that the synthetic gene could be used as an easy way to produce the antigenic vaccine candidate for control of virus-associated diseases or to develop antibodies for diagnostic purpose.

• Korean Journal of Plant Resources
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• v.32 no.2
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• pp.124-143
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• 2019

This study was carried out to build a database system for amylose and protein contents of rice germplasm based on NIRS (Near-Infrared Reflectance Spectroscopy) analysis data. The average waxy type amylose contents was 8.7% in landrace, variety and weed type, whereas 10.3% in breeding line. In common rice, the average amylose contents was 22.3% for landrace, 22.7% for variety, 23.6% for weed type and 24.2% for breeding line. Waxy type resources comprised of 5% of the total germplasm collections, whereas low, intermediate and high amylose content resources share 5.5%, 20.5% and 69.0% of total germplasm collections, respectively. The average percent of protein contents was 8.2 for landrace, 8.0 for variety, and 7.9 for weed type and breeding line. The average Variability Index Value was 0.62 in waxy rice, 0.80 in common rice, and 0.51 in protein contents. The accession ratio in arbitrary ranges of landrace was 0.45 in amylose contents ranging from 6.4 to 8.7%, and 0.26 in protein ranging from 7.3 to 8.2%. In the variety, it was 0.32 in amylose ranging from 20.1 to 22.7%, and 0.51 in protein ranging from 6.1 to 8.3%. And also, weed type was 0.67 in amylose ranging from 6.6 to 9.7%, and 0.33 in protein ranging from 7.0 to 7.9%, whereas, in breeding line it was 0.47 in amylose ranging from 10.0 to 12.0%, and 0.26 in protein ranging from 7.0 to 7.9%. These results could be helpful to build database programming system for germplasm management.

• Korean Journal of Food Science and Technology
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• v.22 no.3
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• pp.343-349
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• 1990

The solubility of protein and phytate was measured at various pH's in distilled water and at various concentrations of NaCl, $CaCl_2\;and\;Na_2SO_3$ solutions, and then optimum condition for producing low phytate protein isolate from perilla flour was investigated. The protein solubility in water showed minimum at pH 4.0 and increased at pH higher or lower than 4.0, while phytate solubility was highest at pH 5.0 and decreased at pH higher or lower than 5.0. In NaCl solution, protein solubility was lowest between pH 3.0-4.0, while phytate solubility was high between pH 2.0-5.0 and abruptly decreased above PH 6.0. In $Na_2SO_3$ solution, protein solubility was lowest between pH 2.0-3.0 and phytate solubility showed maximum values between pH $5.0{\sim}6.0$, and it's solubility was low in 3% salt concentration at all pH ranges. In $CaCl_2$ solution, protein solubility in 3% salt concentration was relatively low at all pH ranges, and phytate solubility showed highest values between pH $2.0{\sim}3.0$ and abruptly decreased (1.0%) above pH 4.0. In order to make low phytate protein isolate, defatted perilla flour protein was extracted at pH9.0 and precipitated at pH 4.0 in 3% NaCl solution. The yield of low phytate protein isolate was 61.4% of total protein. This protein was found to contain 0.02% phytate by weight.

• Korean Journal of Food Science and Technology
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• v.24 no.3
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• pp.284-288
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• 1992

This study was undertaken to investigate the effect of pH and phytate level on the solubility of the protein due to binding between phytate and low-phytate rapeseed protein isolate by means of SDS-polyacrylamide gel electrophoresis. Results showed that the number of protein bands decreased by the increasing amount of phytate added to the soluble extract at pH 2.0 and 5.0 whereas there was no change at pH 11.5. Among 18 bands of rapeseed proteins at pH 2.0, seven bands (105.8, 52.3, 37.3, 34.8, 26.3, 21.3, 18.4 KDa) were removed by precipitation with 100 mg phytate addition and six bands (78.8, 46.5, 19.4, 16.8, 11.7, 8.5 KDa) further disappeared by 150 mg phytate addition. Among 15 bands at pH 5.0, only four bands disappeared by phytate addition. It is suggested that the functionality of rapeseed protein isolate can be improved by lowering the phytate content.