In this experiment forty-eight Sprague Dawley male rats were chosen and used in order to measure the growth rates and to see the effects of lead acumulation in their organs resulting from variously controlled lead protein diet. Protein sources were casein and isolated soyprotein (ISP), and each source was divided into three groups : 7% low protein [LP], 20% standard protein (SP) and 40% high protein (HP) groups. The six experimental groups were given lead acetate(25 mg/kg B.W.) and six control groups were given sodium chloride by oral administration 6 times a week for weeks. The results from this experiment were summeraized as following ; 1) Food consumption, weight gain, organ weight and food efficiency ; Lead acetate administration with protein source had no effects on food consumption, weight gain and organ weight . By their different levels of protein, food consumption of LP group was less the that of SP and HP groups after 3 weeks, weight gain of LP group was less than that of SP and HO groups after 1 weeks. The organ weight in LP group was significantly lower than SP and HP groups except teeth and adrenal s. Effect of lead acetate administration on food efficiency have significantly lower in LP-ISP diet and HP -casein diet than other groups only first week. By their different levels LP group showed significantly lower than SP group until 3 weeks. 2) Hematopoietic effect ; The hematopoieteic effect was not influencec by lead acdtate administration and protein source. But the LP group showed a significantly lowe hematopoietic effect than the SP, HP, groups. 3) Accumulation of lead in the liver, kidney, teeth by protein source showed no significantly differences. Accumulation of lead in blood, heart of LP group, spleen of LP and HP groups. femur of SP and HP groups fed with casein diet groups were significantly higher than fed with ISP diet groups. By their different levels of group showed generally higher than SP and HP groups. But accumulation of lead in teeth of HP group was high also.
The experiment was carried out to study the profile of uterine specific protein during early pregnancy in sows and to test it's immunosuppressive activity. Uterine protein samples were obtained by flushing the uterine horn on Day 3, 6, 9, 12 and 15 of the estrous cycle and the pregnancy respectively and the protein concentration of each sample was determined. The change of uterine protein was examined by sodium dodecyl sulfate(SDS)-PAGE. The immunosuppressive activity of uterine secretory protein was investigated according to the lymphocyte blastogenesis response to mitogen. The results of this experiment are summarized as follows ; 1. The uterine protein during estrous cycle and early pregnancy was relatively constant up to Day 9, but increased on Day 12. Maxium total protein values were found on Day 15. The concentration of serum proteins were about 82-95 mg during estrous cycle, but decreased to about 70-82 mg during early pregnancy. 2. The proteins components similar electrophoretic patterns(PAGE) that were no differences (band ; a, b, c, d, e, f, g, I) on Days 3, 6 and 9 of the estrous cycle and pregnancy. But there were more 2 bands specifically on Day 12 of the pregnancy and on Day 15 of estrous cycle and showed more 4 bands on Day 15 of early pregnancy. They seemed to be acidoprotein and their average molecular weight were 38,000, 22,300 and 12,600. 3. When uterine protein were added 500$\mu\textrm{g}$/ml, there was no immunosuppresive activity on Day 3 of estrous cycle and lymphocyte blastogenesis was slightly suppressed on Day 3 of pregnancy. The immunosuppressive activity on Day 9 of estrous cycle and pregnancy appeared in 500$\mu\textrm{g}$/ml and 150$\mu\textrm{g}$/ml, respectively the uterine protein on Day 12 and 15 showed immunosuppresive activity, which at the level of 150$\mu\textrm{g}$/ml during non-pregnancy and at the level of 100 to 125$\mu\textrm{g}$/ml during early pregnancy, respectively.
Foot-and-Mouth Disease (FMD) is a highly contagious trans-boundary viral disease caused by FMD virus, which causes huge economic losses. FMDV infects cloven hoofed (two-toed) mammals such as cattle, sheep, goats, pigs and various wildlife species. To control the FMDV, it is necessary to understand the life cycle and the pathogenesis of FMDV in host. Especially, the protein-protein interaction between FMDV and host will help to understand the survival cycle of viruses in host cell and establish new therapeutic strategies. However, the computational approach for protein-protein interaction between FMDV and pig hosts have not been applied to studies of the onset mechanism of FMDV. In the present work, we have performed the prediction of the pig's proteins which interact with FMDV based on RNA-Seq data, protein sequence, and structure information. After identifying the virus-host interaction, we looked for meaningful pathways and anticipated changes in the host caused by infection with FMDV. A total of 78 proteins of pig were predicted as interacting with FMDV. The 156 interactions include 94 interactions predicted by sequence-based method and the 62 interactions predicted by structure-based method using domain information. The protein interaction network contained integrin as well as STYK1, VTCN1, IDO1, CDH3, SLA-DQB1, FER, and FGFR2 which were related to the up-regulation of inflammation and the down-regulation of cell adhesion and host defense systems such as macrophage and leukocytes. These results provide clues to the knowledge and mechanism of how FMDV affects the host cell.
Foot-and-mouth disease virus (FMDV) is a small single-stranded RNA virus which belongs to the family Picornaviridae, genus Apthovirus. It is a principal cause of FMD which is highly contagious in livestock. In a wild type virus infection, infected animals usually elicit antibodies against structural and non-structural protein of FMDV. A structural protein, VP1, is involved in neutralization of virus particle, and has both B and T cell epitopes. A RNA-dependent RNA polymerase, 3D, is highly conserved among other serotypes and strongly immunogenic, therefore, we selected VP1 and 3D as vaccine targets. VP1 and 3D genes were codon-optimized to enhance protein expression level and cloned into mammalian expression vector. To produce recombinant protein, VP1 and 3D genes were also cloned into pET vector. The VP1 and 3D DNA or proteins were co-immunized into 5 weeks old BALB/C mice. Antigen-specific serum antibody (Ab) responses were detected by Ab ELISA. Cellular immune response against VP1 and 3D was confirmed by ELISpot assay. The results showed that all DNA- and protein-immunized groups induced cellular immune responses, suggesting that both DNA and recombinant protein vaccine administration efficiently induced Ag-specific humoral and cellular immune responses.
The aim of present study was to elucidate whether the expression of nm23 protein might be of clinical value as a prognostic factor in gastric cancer. The expression of nm23 protein was analyzed using an immunohistochemical method with formalin-fixed and paraffin embedded tissue samples from 76 gastric carcinoma patients. The cytoplasmic immunoreactivity of nm23 protein were detected in 53.9% of the sample tissues(41/76). When the immunoreactivity of nm23 protein with TNM status and other histopathologic findings were compared by using Chi-Square test, nm23 was found to have correlations with lymph node metastasis(p=0.04), a number of metastatic lymph node, and the invasion of lymphatic vessels(p=0.007); however, it had no correlation with TNM status. The conventional prognostic factors such as the depth of invasion, the degree of lymph node metastasis and the presence of distant metastasis, a Borrmann type, size of tumor, and the curability with operation were found to have a strong correlation with the survival time(p<0.003). However, the expression of nm23 protein was not significantly correlated with survival time in survival analysis. These results showed that the expression of nm23 protein is not a useful prognostic indicator in gastric cancer.
Min, Cheol Woo;Gupta, Ravi;Truong, Nguyen Van;Bae, Jin Woo;Ko, Jong Min;Lee, Byong Won;Kim, Sun Tae
Journal of Plant Biotechnology
/
v.47
no.3
/
pp.209-217
/
2020
The presence of high amounts of seed storage proteins (SSPs) improves the overall quality of soybean seeds. However, these SSPs pose a major limitation due to their high abundance in soybean seeds. Although various technical advancements including mass-spectrometry and bioinformatics resources were reported, only limited information has been derived to date on soybean seeds at proteome level. Here, we applied a tandem mass tags (TMT)-based quantitative proteomic analysis to identify the significantly modulated proteins in the seeds of two soybean cultivars showing varying protein contents. This approach led to the identification of 5,678 proteins of which 13 and 1,133 proteins showed significant changes in Daewon (low-protein content cultivar) and Saedanbaek (high-protein content cultivar) respectively. Functional annotation revealed that proteins with increased abundance in Saedanbaek were mainly associated with the amino acid and protein metabolism involved in protein synthesis, folding, targeting, and degradation. Taken together, the results presented here provide a pipeline for soybean seed proteome analysis and contribute a better understanding of proteomic changes that may lead to alteration in the protein contents in soybean seeds.
Kjeldahl method used in many materials from various plant parts to determine protein contents, is laborious and time-consuming and utilizes hazardous chemicals. Near-infrared (NIR) reflectance spectroscopy, a rapid and environmentally benign technique, was investigated as a potential method for the prediction of protein content. Near-infrared reflectance spectra(1100-2400 nm) of coarse cereal grains(n=100 for each germplasm) were obtained using a dispersive spectrometer as both of grain itself and flour ground, and total protein contents determined according to Kjeldahl method. Using multivariate analysis, a modified partial least-squares model was developed for prediction of protein contents. The model had a multiple coefficient of determination of 0.99, 0.99, 0.99, 0.96 and 0.99 for foxtail millet, sorghum, millet, adzuki bean and mung bean germplasm, respectively. The model was tested with independent validation samples (n=10 for each germplasm). All samples were predicted with the coefficient of determination of 0.99, 0.99, 0.99, 0.91 and 0.99 for foxtail millet, sorghum, millet, adzuki bean and mung bean germplasm, respectively. The results indicate that NIR reflectance spectroscopy is an accurate and efficient tool for determining protein content of diverse coarse cereal germplasm for nutrition labeling of nutritional value. On the other hands appropriate condition of cereal material to predict protein using NIR was flour condition of grains.
Lee Bong-Choon;Hong Yeon-Kyu;Hong Sung-Jun;Park Sung-Tae
Research in Plant Disease
/
v.12
no.1
/
pp.25-27
/
2006
Rice dwarf phytoreovirus (RDV), a member of the family Reoviridae has a genome composed of 12 segmented dsRNAs designated as 51 to 512 with an increasing order of mobility in polyacrylamide gel electrophoresis (PAGE). RDV encode 12 structural and non-structural proteins, $P1{\sim}P12$ which are encoded by the $S1{\sim}S12$ segments of the dsRNA genome, respectively. In this experiment, we confirmed in situ localization of RDV particles and P12 in cytoplasm of infected rice plant. We observed specific reaction of the gold particles using virus particle and P12 protein specific antiserum with protein A-gold immunolabelling in electron microscope. It was observed that gold particles specifically react to virus particles in cytoplasm in case using the antiserum for virus particles. In the case of antiserum for P12 protein, gold particles sporadically existing on cytoplasm without existing in organelle of cytoplasm specifically. As this result, RDV P12 protein encoded by S12 located in cytoplasm.
Formation of adduct was studied in benzo(a)pyrene(BP)- and doxorubicin(Dx)-treated human NC-37 cells and isolated nuclei. Major adducts formed were determined by fluorescence absorption spectrophotometery and DNA-lin-ked protein assay. When isolated nuclei were exposed to carcinogens BP and DMBA, and anticancer drugs m-AMSA, ellipticine and Dx, varying degrees of adduct formation occured between DNA-protein complex and these drugs. When the mixture was centrifuged 1.7 M sucrose solution, binding BP and DMBA appeared to be similar between the sediment and the supernatant. When the sediment was centrifuged again with 0.35% polymin-P, the amount of BP bound was 2-fold greater in the protein(1077$\pm$55cpm) than in DNA fraction (470$\pm$20cpm), whereas that of DMBA was 1.6-fold greater in the DNA than in protein fraction. In the case of m-AMSA, ellipticine and Dx, the amount of binding was slightly greater in supernatant than in sediment in centrifugation with 1.7 M sucrose, and more than 3 times greater in the DNA- than in protein- fraction in centrifugation with 0.35% polymin P. DNA fractions which associated with a subset of nonhistone chromosomal protein were isolated from NC-37 cells exposed to $^{3}$H-BP and $^{14}$C-Dx. They were separated into two distince components DNA-S and DNA-P by centrifugation with 2M Nacl chromatin extraction. The results indicated that the amount of $^{3}$H-BP bound was 6.0-fold greater in DNA-P as compared with DNA-S, while that of $^{14}$C-Dx binding appreaed to be 6.2-fold greater in DNA-S than in DNA-P fraction. When $^{3}$H-BP binding wasdetermined in the presence of cold Dx, the amount of binding was reduced only in the DNA-P fraction, indicating that the interaction between DNA and protein is decreased. Gene expression by these drugs, BP treated cells were increased to compare with nomal cells but reduced by treatment with BP-Dx. These results suggest that the protein moiety which tightly bound to DNA-P fraction may play an important role in the regulation of gene expression.
We have found a protein kinase activity that is tightly associated with type II DNA topoisomerase purified from regenerating rat liver. The activities of protein kinase and topoisomerase II were not separable when the enzyme was subjected to analytical chromatographies (Hydroxyapatite, phosphocellulose, and double strand DNA cellulose) and glycerol gradient sedimentation. The kinase activity from purified rat topoisomerase II was also inactivated by the topoisomerase II inhibitors such as N-ethylmaleimide or novobiocin. The evidences, however, do not rule out a possibility that the kinase activity resides in a polypeptide other than the topoisomerase II protein. The topoisomerase II-associated protein kinase required Mg++ for its activity, and this requirement was not substituted by any other mono- or divalent ions. Histone H1 act as a strong stimulator and a good substrate for the kinase activity and other histones and ${\alpha}$-casein could not substitute the effect of histone H1.
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