• BMB Reports
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• 제40권1호
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• pp.65-71
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• 2007

The Helicoverpa armigera nucleopolyhedrovirus (HearNPV) ORF80 (ha80) has 765 bp encoding a protein with approximately 254 amino acids and a predicted molecular weight of 30.8 kDa. Homologues of ha80 are found in most baculovirus sequences, including those from lepidopteran NPVs, lepidopteran granuloviruses (GVs), hymenopteran baculoviruses, and one dipteran baculovirus, yet their functions remain unclear. In this study we characterized ha80, and showed that it was transcribed late in infected host cells (HzAM1). The product of ha80 was a 31 kDa protein that was not a structural protein of budded virus (BV) or occlusion-derived virus (ODV) particles. Ha80 was first detected in the cytoplasm of infected HzAM1 cells at 12 h p.i., and was observed in the nucleus at later stages of infection, suggesting that it may be involved in transporting viral proteins into the host cell nucleus or play its roles in the nucleus.

• 대한약리학회지
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• 제31권2호
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• pp.241-250
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• 1995

Protein B23 is one of the major nucleolar phosphoproteins associated with pre-ribosomal particles, and is localized in the granular region of the nucleolus. Recent studies suggest that protein B23 shuttles between nucleus and cytoplasm and also interacts with HIV Rev. These findings indicate that protein B23 is important in nucleocytoplasmic relationship and viral replication. However, the exact function of protein B23 is not clear yet. In acute nucleolar hypertrophy of rat liver, treated with thioacetamide, there was observed an increase of not only protein B23 but also B23-like protein p45 when anti-B23 monoclonal antibody (MAb) was used for identification. On the basis of the large B23 specific epitope structure composed of 68 amino acids, a hypothesis was formulated to examine that p45 is the pre-B23 resulting from excessive production of B23. In an attempt to investigate the precursor of B23, we analyzed the subcellular fractions and microsomal subfractions. Subsequently, we analyzed the finger printings of B23-like proteins using the tryptic peptide mapping. The results are summarized: 1) Using B23 MAb, we observed the presence of B23-like proteins in nucleolar fraction, nucleoplasmic fraction and microsomal fraction. 2) In the further microsomal subfractionation, we could partially purify B23-like protein in 2M layer of sucrose gradient. 3) When ion exchange chromatography was employed, there were protein species 80kDa(p80), 65kDa(p65) and 60kDa(p60). 4) Based on the tryptic map analysis of $^{125}I$ labeled proteins, the similarity between B23 and p80 was found only in 9 out of 14(B23) and 21(p80) peptides, and difference was found in the remaining peptides. p80 and p60 had 18 common peptides, and all the peptides of p60 were similar to those of p80. From these results, it is proposed that p45 is an abnormal metabolite resulting from carcinogenesis by thioacetamide, and it is not the precursor of B23. In addition, we suggest that p80 may be a precursor of p45.

• 한국잠사곤충학회지
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• 제41권2호
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• pp.75-81
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• 1999

The storage protein-like protein has been purified from the 5th instar larval haemolymph of the Chinese osk silkwom, Antheraea pernyi, and the preparation was shown to be homogeneous by 7.5% native-PAGE. The molecule was consisted of a single subunit with a molecular weight of 80K, but the number of the subunits was not determined. The protein was defied as glycoprotein by Schiff's regent stining. Rabbit antibody prepared against the purified protein crotein crossreacted with the 5th instar larval haemolymph proteins of Antheraea pernyi and antheraea yamamai, but not with those of Bombyx mori and Bombyx mandarina.

• Nutrition Research and Practice
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• 제4권5호
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• pp.375-382
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• 2010

The precise effects of protein intake on fractional synthesis rate (FSR) of muscle protein are still under debate. The sample size of these studies was small and the conclusions in young and elderly subjects were inconsistent. To assess the effect of dietary protein intake on the FSR level, we conducted a meta-analysis of controlled protein intake trials. Random-effects models were used to calculate the weighted mean differences (WMDs). Ten studies were included and effects of short-term protein intake were evaluated. In an overall pooled estimate, protein intake significantly increased the FSR (20 trials, 368 participants; WMD: 0.025%/h; 95%CI: 0.019-0.031; P < 0.0001). Meta-regression analysis suggested that the protein dose was positively related to the effect size (regression coefficient = 0.108%/h; 95%CI: 0.035, 0.182; P = 0.009). A subgroup analysis indicated that protein intake significantly increased FSR when the protein dose was ${\leq}$ 0.80 g/kg BW (16 trials, 308 participants; WMD: 0.027%/h; 95%CI: 0.019-0.031; P < 0.0001), but did not affect FSR when the protein dose was > 0.80 g/kg BW (4 trials, 60 participants; WMD: 0.016%/h; 95%CI: 0.004-0.029; P = 0.98). In conclusion, this study is the first integrated results showing that a short-term protein intake is effective at improving the FSR of muscle protein in the healthy elderly as well as young subjects. This beneficial effect seems to be dose-dependent when the dose levels of protein range from 0.08 to 0.80 g/kg BW.

• 한국어병학회지
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• 제22권2호
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• pp.173-177
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• 2009

Lymphocystis disease virus (LCDV) was detected from olive flounder Paralichthys olivaceus, painted glass fish Chanda baculis, gourami Trichogaster leeri and rockfish Sebastes schlegeli, and proteins of the viruses were compared. The major capsid protein (MCP) gene-specific primer sets successfully amplified approximately 1300 bp nucleotides from the olive flounder and 600 bp nucleotides from painted glass fish, gourami and rockfish isolates, respectively. In western blotting analysis using anti-LCDV mouse polyclonal serum, major antigenic proteins had 21, 26, 45, 50, 80, 110 and 120 kDa in olive flounder, 26, 47 and 80 kDa in painted glass fish, 26, 46, 80 and 92 kDa in gourami, 26, 44, 49, 80 and 105 in rockfish, respectively. All the marine and freshwater isolates showed only common antigens of approximately 26 kDa and 80 kDa. These results suggest that antigenic protein profiles of LCDVs may vary depending upon fish species.

• 한국양식학회지
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• 제12권4호
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• pp.293-301
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• 1999

This study was conducted to evaluate the possible utilization of 5 different animal protein sources in juvenile rainbow trout, Oncorhynchus mykiss. Meat and bone meal (MBM), feather meal (FM), squid liver powder (SLP), poultry by-product(PBP) and blood meal (BM) were chosen to be the candidate for the possible ingredients for the dietary fish meal replacer in rainbow trout feed. Six different diets were formulated of isonitrogenous and isocaloric basis of $48\textperthousand$ crude protein and 16.7 kJ/g diet: diet 1, $100\textperthousand$ white fish meal (WFM); diet w, $80\textperthousand$ WFM +20% MBM; diet 3, 80% WFM +20% FM; diet 4, 80% WFM+20% SLP; diet 5, 80% SFM+20% PBP; diet 6, 80% WFM +20% BM. As the dietary protein sources, each diet containing 34.7% of animal protein were supplied by WFM with and without MBM, FM, SLP, PBP or BM and approximately 64.2% of plant protein. After one week of conditioning period, fish averaging 2g were divided into six groups and fed one of the experimental diets for 8 weeks. After eight weeks of feeding trials, there were no significant differences in weight gain and feed conversion ratio among groups of fish fed diet 1, 3, 4, 5 and 6(P>0.05). However, weight gain of fish fed diet 2 were significantly lower than those of fish fed diet 1, 3, 4, 5 and 6(P<0.05). These results indicated that FM, SLP, PBP and BM can be used as a dietary fish meal replacer up to 20% in juvenile rainbow trout.

• Journal of Nutrition and Health
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• 제5권3호
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• pp.135-140
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• 1972

Rice and other corns as well as potato were mixed, as indicated in the following table, and fed to the experimental animals for 14 weeks. It was observed that the 9th and 10th dietary groups, whose protein values were higher among the experimental groups, displayed the more ideal growth and development as compared with other groups, and that the mixing ratio in these groups was proved to be better nutritionally as judged from the serum protein levels. Ratio of food Mixture Control Standard diet : Group 1 rice 80% Barley 20% Group 2 rice 80% Wheat 20% Group 3 rice 100% Group 4 rice 80% millet 20% Group 5 rice 80% Potato 20% Group 6 rice 80% Barley 20% Group 7 rice 80% Potato 10% Barley 10% Group 8 rice 80% Barley 10% Potato 10% Group 9 rice 80% Soybean 10% Potato 10% Group 10 rice 80% Soybean 10% Barley 10%(wheat 10%)

• 한국임상수의학회지
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• 제21권3호
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• pp.253-258
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• 2004

DNA double-strand break (DSB) is a serious treat for the cells including mutations, chromosome rearrangements, and even cell death if not repaired or misrepaired. Ku heterodimer regulatory DNA binding subunits (Ku70/Ku80) bound to double strand DNA breaks are able to interact with 470-kDa DNA-dependent protein kinase catalytic subunit (DNA-PKcs), and the interaction is essential for DNA-dependent protein kinase (DNA-PK) activity. The Ku80 mutants were designed to bind Ku70 but not DNA end binding activity and the peptides were treated in breast cancer cells for co-therapy strategy to see whether the targeted inhibition of DNA-dependent protein kinase (DNA-PK) activity sensitized breast cancer cells to ionizing irradiation or chemotherapy drug to develop a treatment of breast tumors by targeting proteins involved in damage-signaling pathway and/or DNA repair. We designed domains of Ku80 mutants, 26 residues of amino acids (HN-26) as a control peptide or 38 (HNI-38) residues of amino acids which contain domains of the membrane-translocation hydrophobic signal sequence and the nuclear localization sequence, but HNI-38 has additional twelve residues of peptide inhibitor region. We observed that the synthesized peptide (HNI-38) prevented DNA-PKcs from binding to Ku70/Ku80, resulting in inactivation of DNA-PK complex activity in breast cancer cells (MDA-465 and MDA-468). Consequently, the peptide treated cells exhibited poor to no DNA repair, and became highly sensitive to irradiation or chemotherapy drugs. The growth of breast cancer cells was also inhibited. These results demonstrate the possibility of synthetic peptide to apply breast cancer therapy to induce apoptosis of cancer cells.

• 한국식품영양학회지
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• 제17권1호
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• pp.66-71
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• 2004

백삼단백질의 가열에 의한 내열특성을 알아보기 위하여 가열시간에 따른 내열성 단백질의 함량과 전기영동패턴을 조사하고, CM-cellose 컬럼크로마토그라피 방법으로 얻어진 분획을 가열하여 내열성 단백질과 비내열성단백질의 이온성분의 단백질함량을 분석하고 분자량을 확인하였다. 그 결과 가열시간에 따른 내열성 단백질의 함량은 주근 중심이 주근 주피보다 전체적으로 높았으며 두부위 모두 가열시간이 90분 이후부터는 감소하는 경향이 커졌다, 가열시간에 따른 내열성 단백질량은 가열시간이 길어짐에 따라 단백질은 감소하였고, 가열시간 30분까지는 66, 45, 29, 24, 22, 20, 12 kD 등 7개의 밴드가 가열시간 60분부터는 분자량 22 kD는 소실되었음이 확인되었다. 단백질 함량은 내열성 단백질이 비내열성 단백질보다 높게 나타났으며, 내열성 단백질 함량은 양이온성 단백성분 분획이 28.24%로 음이온성 단백성분 0.80%보다 훨씬 높았다. 내열성 단백질의 분자량은 66, 55, 36 kD 임을 확인하였다.

• Asian-Australasian Journal of Animal Sciences
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• 제15권5호
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• pp.732-739
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• 2002

Milk samples with different phenotype combination of $\{kappa}$-casein and ${\beta}$-lactoglobulin and different preheating temperatures of 30, 70, 75 and $80^{\circ}C$ were used for cheesemaking under laboratory conditions. For the 853 batches of cheese, mean composition was 59.64% total solids, 30.24% fat and 23.66% protein, and the whey contained 6.93% total solids, 0.30% fat and 0.87% protein. Least squares analysis of the data indicated that heating temperature of the milk and ${\kappa}$-CN/${\beta}$-LG phenotypes had significant effects on cheese and whey compositions. The total solids, fat and protein contents of cheese were negatively correlated with preheating temperatures of milk. Cheese from BB/BB phenotype milk had the highest and those from AA/AA phenotype milk had the lowest concentrations of total solids, fat and protein. Mean recoveries of milk components in the cheese were 53.71% of total solids, 87.15% of fat, and 80.32% of protein. For the 10 different types of milk, maximum recoveries of milk components in cheese occurred with preheating temperature of $70^{\circ}C$ or $75^{\circ}C$ and lowest recoveries occurred at $80^{\circ}C$. The whey averaged 6.94% total solids, 0.30% fat and 0.87% protein. Losses of milk components in the whey were lowest for milk preheated at $80^{\circ}C$ and for milk containing the BB/BB phenotype.