• Korean Journal of Veterinary Research
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• v.50 no.4
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• pp.285-295
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• 2010

Protein expression patterns in Salmonella enterica subspecies enterica serovar Typhimurium (S. Typhimurium) strains with diverse phenotypes, such as phage type, antibiotic resistance pattern and plasmid profiles were examined. For detailed analysis of proteins expressed by different S. Typhimurium strains, protein fractions were divided into detergent-rich phase (DP) and aqueous phase (AP) using triton X-114 detergent. The two phases were subjected to two-dimensional gel electrophoresis (2-DE), followed by protein identification using peptide mass fingerprinting (PMF). In the results, PMF showed that DP fractions consisted mainly of outer membrane proteins, whereas the AP fractions included cytosolic proteins. Comparison of 2-DE profiles of DP did not show any distinct protein spots which could be correlated with phage type, antibiotic resistance pattern or plasmid profile. However, comparisons of 2-DE profiles of the AP revealed differences in the protein spots, which could be correlated with the plasmid profile and phage types. Among these protein spots, flagellin was specific for strains containing a 90 kb plasmid. Compared to DT193 phage type, three protein spots in the range of pI 5.0-5.5 and MW 8-15 kDa of AP 2-DE profiles were absent in the DT104 phage types. Additionally, a protein spot with PI in the range of 4.5-5.0 and molecular weight (MW) between 51-69 kDa was specific for phage type DT104, while a protein spot with pI in the range of 4.0-4.8 and MW between 18-20 kDa was specific for DT193 phage type. These protein spots may be useful for discriminating phage types of S. Typhimurium.

• Journal of the Korean Society of Food Culture
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• v.34 no.6
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• pp.779-784
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• 2019

The purpose of this study was to optimize the rice protein extracted using a response surface methodology. The experiment was designed based on a CCD (Central Composite Design), and the independent variables were the high pressure (X₁, 0-400 MPa) and processing time (X₂, 0-10 minutes). The results of the extraction content (Y₁), residue content (Y₂), and recovery yield (Y₃) were fitted to a response surface methodology model (R²= 0.92, 0.92, and 0.93, respectively). Increasing the pressure and processing time has a positive effect on the extraction content (Y₁), residue content (Y₂), and recovery yield (Y₃). Therefore, these high-pressure conditions (independent variables) can significantly affect the improvement in rice protein extraction efficiency. Thus, the optimal conditions of X₁ and X₂ were 400 MPa and 10 min., respectively. Under these optimal conditions, the predicted values of Y₁, Y₂, and Y₃ were 62.93, 57.53 mg/g, and 91.76%, respectively.

• The Korean Journal of Zoology
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• v.28 no.1
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• pp.21-30
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• 1985

By two-dimensional gel electrophoresis loss of a cell-specific protein was detected in tD strain of Amoeba proteus that had been infected by symbiotic bacteria extracted from xD strain. In 50 days of experimental infection by induced phagocytosis the host amoeba lost the ability to synthesize the tD cell-specific protein even after removal of the infective bacteria and xD cell-specific protein by growing the amoebae at $27^\\circC$. By this time the host amoebae were obligately dependent on the bacteria. From these and other results (Lorch and Jeon, Science 221:549), it is clear that the incompatibility of the infected nuclei with the cytoplasm of the uninfected amoeba and the obligate dependence of the host on bacteria are due to the irreversible inactivation or the loss of the cell-specific gene by bacterial infection in this amoeba.

• BMB Reports
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• v.52 no.5
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• pp.304-311
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• 2019

The cytoplasmic FMR1-interacting protein family (CYFIP1 and CYFIP2) are evolutionarily conserved proteins originally identified as binding partners of the fragile X mental retardation protein (FMRP), a messenger RNA (mRNA)-binding protein whose loss causes the fragile X syndrome. Moreover, CYFIP is a key component of the heteropentameric WAVE regulatory complex (WRC), a critical regulator of neuronal actin dynamics. Therefore, CYFIP may play key roles in regulating both mRNA translation and actin polymerization, which are critically involved in proper neuronal development and function. Nevertheless, compared to CYFIP1, neuronal function and dysfunction of CYFIP2 remain largely unknown, possibly due to the relatively less well established association between CYFIP2 and brain disorders. Despite high amino acid sequence homology between CYFIP1 and CYFIP2, several in vitro and animal model studies have suggested that CYFIP2 has some unique neuronal functions distinct from those of CYFIP1. Furthermore, recent whole-exome sequencing studies identified de novo hot spot variants of CYFIP2 in patients with early infantile epileptic encephalopathy (EIEE), clearly implicating CYFIP2 dysfunction in neurological disorders. In this review, we highlight these recent investigations into the neuronal function and dysfunction of CYFIP2, and also discuss several key questions remaining about this intriguing neuronal protein.

• Bulletin of the Korean Chemical Society
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• v.33 no.9
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• pp.3091-3094
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• 2012

• Journal of Animal Science and Technology
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• v.51 no.2
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• pp.155-162
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• 2009

This study was conducted to determine the protein requirement level in adult Jindo dog (Korea Jindo Dog) through nitrogen balance experiments. 12 female dogs aged 36~38 weeks old (for early stage) or aged 45~49 weeks old (for late stage) were fed one of 3 diets containing 17, 19 and 21% of crude protein. Body weight of dogs were measured during the 12 days of feeding trial, and feces and urine were collected last 3 days of the trial period. In early stage of Jindo dog, average daily gain of dogs fed experimental diets containing 17, 19 and 21% of crude protein were -38.33, -16.25 and -12.71g/d, respectively. There was a significant differences between 17 and 21% of crude protein treatments (p<0.05) and calculated retained nitrogen were -0.29, -0.04 and -0.03g/kg$BW^{.75}$/d, respectively. In late stage of Jindo dog, average daily gain of dogs fed experimental diets containing 17, 19 and 21% of crude protein were -34.05, -28.71 and -28.28g/d, and calculated retained nitrogen were -0.33, -0.06 and 0.09g/kg$BW^{.75}$/d, respectively, and were significantly higher (p<0.05) in dogs fed 21% of crude protein diet than those of other dogs. In early stage and late stage of adult Jindo dog, a calculated linear regression equation for nitrogen intake (x) and nitrogen retention (y) were y = 0.7484x-1.18 ($R^2$ = 0.9923) and y = 0.88231x-1.0894 ($R^2$ = 0.9982) and the requirement of crude protein were estimated as 9.85g/kg$BW^{.75}$/d and 7.72g/kg$BW^{.75}$/d from above equation.

• The Korean Journal of Physiology
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• v.3 no.2
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• pp.9-16
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• 1969

It is well known that a number of -SH and -SS containing substances afford a certain measure of protection against radiation effects in many biological systems, and it is conceivable that inherent -SH levels in Ehrlich ascites tumour (ELD)cells may be of decisive improtance with respect to the development of cellular radiation injury. So far, little effort has been directed to elucidate the changes in levels of different -SH and -SS groups in ELD cells when the tumour-bearing whole animal was subjected to the sublethal dose of X-irradiation. The present study was designed to bring some lights in the possible changes of and relationship between various sulfhydryl levels, such as P-SH, NP-SH and NP-SS, as well as the content of protein and cell volume of ELD cells, after subjecting the ELD mice to 1,200 r of X-irradiation. The animals used in this experiment were all mixed bred mice of $20{\sim}25\;gm$ in body weight (approximately 2 months old) irrespective of sex. 12 mice in one experiment were inoculated intraperitoneally with 0.2 ml of ascites tumour cells $(2{\times}10^6\;cells)$, and on the 7th day of the tumour growth, they were X-irradiated with 1,200 r, using the conventional X-ray machine under the following conditions: 200 Kv at 15 mA, 0.5 mm Cu filter, target-skin distance: 50 cm. Radiation dose was measured with the the Philip integrating dosimeter. At 24, 36, 48 and 60 hours after the X-irradiation, the mice were killed by cervical dislocation, and the tumours were taken out. Freshly withdrawn ascites tumours were placed in ice, and immediately the cell concentration was measured with the Coulter Cell Counter (Model B), and the hematocrit of the tumour cells were also determined. Cell volume was thus calculated by the cell concentration and hematocrit value. P-SH content of ELD cells was measured potentiometrically according to the method of Calcutt & Doxey, and NP-SH and NP-SS contents were measured spectrophotometrically by the method described by Ellman. Protein content of ELD cells was determined with the Folin phenol reagent by Lowry et al. Altogether, 48 experimental mice were used, and 12 mice with the only exception of X-irradiation were used as the control. Results obtained indicate that the contents of all the cellular sulfhydryl groups as well as cell volume and protein content of the ELD cells increase significantly as time progresses after the sub-lethal X-ray dose of 1,200 r was given and that all the increase is in a lineal fashion. The regression lines of the relative values, (i. e., taking each control value as 1) of all the values obtained, and the regression lines of cell volume, protein and NP-SH are identical, whereas those of NP-SS and P-SH appear to be widely seperated. However, the difference of those two lines (NP-SS & P-SH) were found to be not significant statistically (p>0.05). Therefore, it can be concluded from the above results that all the values examined increase in a lineal fashion with no statistically significant difference among them. Also, with the radiation dose of 1,200 r, the ELD cell becomes enlarged and swollen progressively up to 60 hours post-irradiation and it becomes more than two times of the original normal size at 60 hours after the irradiation, and up to this stage, it seems apparent that the cell division has been slow due to the X-irradiation applied in this experiment. It is well understandable that the contents of NP-SH, NP-SS, P-SH and protein of the ELD cells increase in parallel with the increase of the cell volume by the X-ray does used, but it also seems interesting to note that all the cellular substances tested show no appreciable difference in the pattern of increase.

• The Korean Journal of Mycology
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• v.20 no.1
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• pp.72-76
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• 1992

The extraction and separation methods of protein-bound polysaccharides from the mycelium and culture broth of Coriolus versicolor (Fr) Quel were investigated. The use of 2% solution of surface active agent Triton X-100, was effective for extraction of the protein-bound polysaccharides from the mycelium. For the separation and partial purification of the protein-bound polysaccharides, the column chromatography using DEAE-Cellulose and DEAE-Sephadex proved to be effective.

• Proceedings of the Korean Society of Crop Science Conference
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• 2022.10a
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• pp.63-63
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• 2022

Wheat flour can be categorized into bread, all-purpose, cake flour according to its protein content. Since optimal wheat flour protein content is different for each end use, it is necessary to diversify the nitrogen fertilizer methods depending on the end use and cultivar. Optimal wheat flour protein content of soft wheat (for cake flour) is lowest (<=10%) among all end use, it is necessary to develop nitrogen fertilizer methods for high yield and low protein content. In order to analyze the yield and quality changes of soft wheat as nitrogen fertilizer amount and splitting timing, soft wheat cultivar 'goso' was sown on paddy soil in jeunju, Republic of Korea ('21.10). the amount of nitrogen fertilizer was divided into 4 levels by adjusting 2kg/10a increments from 5.1 to ll.lkg/lOa, and in the N 7.1 and 9.1 kg/1 Oa(standard) treatment, N amount divided into sowing date:regrowing stage=3:7,4:6(standard), 5:5. In regrowing stage, Tiller number and N fertilizer amount at sowing date showed a correlation; y=-121.14x²+792.66x-525.41 (R²=0.77^*, y: Tiller number/m², x: N amount at sowing date(kg/10a)). Tiller number in regrowing stage was the highest when the nitrogen fertilizer amount at sowing date was 3.23kg/10a. spike number per m² was the highest when N fertilizer was divided into sowing date:regrowing stage=3:7(N amount: 9.1kg/10a). If N fertilizer amount was fixed, grain yield was also the highest when N fertilizer was divided into sowing date :regrowing stage=3:7. Also, N amount at sowing date and grain yield showed no correlation, but N amount at regrowing stage and grain yield showed significant correlation. As N amount increased, protein content also showed a tendency to increase.

• Journal of Plant Biotechnology
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• v.35 no.3
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• pp.177-183
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• 2008

Ac/Ds mutant lines of this study were transgenic rice plants, each of which harbored the maize transposable element Ds together with a GUS coding sequence under the control of a promoterless(Ds-GUS). We selected the mutants that were GUS expressed lines, because the GUS positive lines will be useful for identifying gene function in rice. One of these mutants was identified knock-out at Oszinc626(NP_001049991) gene, encoding a RING-H2 zinc-finger protein, by Ds insertion. In this mutant, while primary root development is normal, secondary root development from lateral root was very poor and seed development was incomplete compare with normal plant. RING zinc-finger proteins play important roles in the regulation of development in a variety of organisms. In the plant kingdom, a few genes encoding RING zinc-finger proteins have been documented with visible effects on plant growth and development. The consensus of the RING-H2(C3-H2-C3 type) domain for this group of protein is $Cys-X_2-Cys-X_{28}-Cys-X-His-X_2-His-X_2-Cys-X_{14}-Cys-X_2-Cys$. Oszinc626 encodes a predicted protein product of 445 amino acids residues with a molecular mass of 49 kDa, with a RING-zinc-finger motif located at the extreme end of the C-terminus. RT-PCR analysis indicated that the expression of Oszinc626 gene was induced by IAA, cold, dehydration, high-salinity and abscisic acid, but not by 2,4-D, and the transcription of Oszinc626 gene accumulated primarily in rice immature seeds, root meristem and shoots. The gene accumulation patterns were corresponded with GUS expression.