• Korean Journal of Fisheries and Aquatic Sciences
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• v.53 no.2
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• pp.165-173
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• 2020

Fish roe is among the most valuable food resources produced by fisheries. Raw fish roe requires processing for conversion into hygienic, marketable, and consumer-acceptable forms. In this study, to investigate the food compositional characteristics of various types of fish roe, we applied vacuum freeze-drying to prepare fish roe concentrates (FRCs) from roe of Alaska pollack Theragra chlcogramma, bastard halibut Paralichythys olivaceus, and skipjack tuna Katsuwonus pelamis. The FRC yield ranged from 22.7 to 26.7 g/100 g roe. The major constituents of FRCs were protein (65.4-79.6%), moisture (2.8-6.2%), lipids (8.5-18.3%), and ash (4.8-7.2%). Potassium, sulfur, sodium, and phosphorus were the major mineral elements of FRCs, and the major amino acids were aspartic acid (9.0-10.4 g/100 g protein), glutamic acid (13.2-14.5 g/100 g protein), lysine (8.4-8.6 g/100 g protein), and leucine (8.3-9.7 g/100 g protein). Vacuum freeze-dried FRCs differed among fish species in terms of amino acid composition and electrophoresis protein band distribution. Therefore, FRCs are an excellent source of protein nutrition and an appropriate protein fortification material in human foods or animal feed.

• Journal of Nutrition and Health
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• v.21 no.2
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• pp.99-112
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• 1988

This study was performed to investigate the effects of dietary protein and calcium levels on calcium metabolism in eight healthy Korean adult females. The 2-day metabolic study consisted of a 2 day adaptation period and three 6-day experimental periods. Three experimental diets were low protein low calcium(LPLCa : protein 44g, Ca 422mg), higher protein low calcium(HPLCa : protein 85g, Ca 365mg), and high protein high calcium (HPHCa : protein 84g, Ca 727mg). The apparent calcium absorption was likely to be affected by the calcium intake rather than by the protein intake. Average calcium absorption rate was about 23-29% of calcium intake. The calcium balance was -21.44mg for LPCa, -25.02mg for HPLCa, and -3.22mg for HPHCa. Avergae urinary calcium excretion was 127.7mg for LPLCa, 108.6mg for HPLCa, and 215.4mg for HPHCa. Urinary calcium excretion was more closely related to the changes of calcium intake rather than of protein intake. These results seemed to be due to the interactions between the high phosphours contained in the high protein diet and the little discrepancy of protein intake levels.

• Journal of Sericultural and Entomological Science
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• v.17 no.2
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• pp.161-170
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• 1975

This study is to investigate the content of crude protein intruded in the sericin of cocoon shell and pupa by treatment of buffer solution (pH 1 to pH 13) 20 ml per 1 gram for 30 and 60 minutes at 30$^{\circ}C$, 60$^{\circ}C$ and 100${\pm}$2$^{\circ}C$, respectively. The results obtained are summarized as follows. 1. The quantity of total crude protein obtained from cocoon shell and pupa by treatment during 30 minutes at 30$^{\circ}C$ was dissolved as the largest quantity of 11.874 mg/g at pH 1 and l5.93mg/g at pH 13, but dissolved the smallest quantity 1.75g/g at pH 5 as known. and tile quantity of crude protein treated for 60 minutes is 13.437mg/g at pH 1 and 22.50mg/g at pH 13. Also, the smallest quantity is 2. 813mg/g at pH 5 as known. 2. By the treatment during 30 minutes at 60$^{\circ}C$, the dissolved largest quantity was 13.12mg/g at pH 1 and 21.875 mg/g at pH 13, but the smallest quantity is 2.375mg/g at pH 5 as known After treatment for 60 minutes at 60$^{\circ}C$, the dissolved largest quantity was 17.500 mg/g at pH 1 and 31.56mg/g at pH 13, bu the smallest quantity is 3.849 mg/g at pH 5. 3. The dissolved crude protein from the cocoon shell and pupa by treatment for 30 minutes at 100${\pm}$2$^{\circ}C$ was the largest quantity of 147.000mg/g at pH 1 and 398. 125mg/g at pH 13, but the smallest quantity is 75.00mg/g at pH 5 as known. After treatment for 60 minutes at 100${\pm}$2$^{\circ}C$, the largest quantity was 253.76 mg/g at pH 1 and 460.625mg/g at pH 13, but the smallest quantity is 139.375mg/g at pH 5 as known. 4. The dissolved crude protein from the cocoon shell and pupa was not different in quantity by treatment at 30$^{\circ}C$ or 60$^{\circ}C$. But dissolved crude protein was large quantity from cocoon shell more than pupa, as known. 5. The treatment of cocoon shell and pupa during 60 minutes at 100${\pm}$20$^{\circ}C$ was increased to the dissolved largest quantity of crude protein of 19.20％ at pH 1 and 22. 18％ at pH 13 from the cocoon shell and 6. 12％ at pH, an d 23.87％ at pH 13 from the pupa. But dissolved crude protein was increased to the larger quantity from pupa more than cocoon shell.

• The Korean Journal of Pain
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• v.19 no.1
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• pp.8-16
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• 2006

The regulators of the G protein signaling (RGS) proteins are responsible for the rapid acceleration of the GTPase-activity intrinsic to the heterotrimeric G protein alpha subunits. As GTPase-activating proteins (GAP), the RGS proteins negatively regulate the G-protein signals. Recently, the RGS proteins are known to be one of the important regulators of opioid signal transduction and the development of tolerance. The aim of this study was to review the recent discovery and understanding of the role of RGS proteins in opioid signaling and the development of tolerance. This information will be useful for medical personnel, particularly those involved in anesthesia and pain medicine, by helping them improve the effective use of opioids and develop new drugs that can prevent opioid tolerance.

• Archives of Pharmacal Research
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• v.28 no.11
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• pp.1275-1281
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• 2005

The $G_{q/11}$ protein-coupled receptors, such as muscarinic (M1 & M3) receptors, have been shown to regulate the release of a soluble amyloid precursor protein (sAPP$\alpha$) produced from $\alpha$-secretase processing. However, there is no direct evidence for the precise characteristics of G proteins, and the signaling mechanism for the regulation of $G_{q/11}$ protein-coupled receptor mediated sAPP$\alpha$ release is not clearly understood. This study examined whether the muscarinic receptor-mediated release of sAPP$\alpha$ is directly regulated by $G\alpha_{q/11}$ proteins. The HEK293 cells were transiently cotransfected with muscarinic M3 receptors and a dominant-negative minigene construct of the G protein $\alpha$ subunit. The sAPP$\alpha$ release in the media was measured using an antibody specific for sAPP. The sAPP$\alpha$ release enhancement induced by muscarinic receptor stimulation was decreased by a $G_{q/11}$ minigene construct, whereas it was not blocked by a control minigene construct (the G$\alpha$ carboxy peptide in random order, G$\alpha_{q}$R) or $G\alpha_{j}$ constructs. This indicated a direct role of the $G\alpha_{q/11}$ protein in the regulation of muscarinic M3 receptor-mediated sAPP$\alpha$ release. We also investigated whether the transactivation of the epidermal growth factor receptor (EGFR) by a muscarinic agonist could regulate the sAPP$\alpha$ release in SH-SY5Y cells. Pretreatment of a specific EGFR kinase inhibitor, tyrophostin AG1478 (250 nM), blocked the EGF-stimulated sAPP$\alpha$ release, but did not block the oxoM­stimulated sAPP$\alpha$ release. This demonstrated that the transactivation of the EGFR by muscarinic receptor activation was not involved in the muscarinic receptor-mediated sAPP$\alpha$ release.

• Journal of Life Science
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• v.19 no.12
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• pp.1731-1736
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• 2009

Recent studies determined that a chronic western-style diet increased the endogenous small heterodimer partner (SHP) protein levels in mice. In experiments with cell cultures, chenodeoxy cholic acid (CDCA) treatment increased endogenous SHP protein levels and reduced the degradation rate of exogenously expressed flag-SHP levels in the human hepatoma cell line, HepG2 cells. In addition, bile acid-induced intestinal fibroblast growth factor-19 (FGF-19) increased the half-life of the exogenously expressed SHP when HepG2 cells were transfected with ad-flag-SHP. However, both the expression level and the degradation rate of the endogenous SHP in response to cholic acid and FGF-19 have not been well understood, either in mice or in cultured HepG2 cells. This study examined the effects of cholic acid treatment on the endogenous SHP protein levels in mice and the effects of FGF-19 on the degradation rate of the endogenous SHP protein in HepG2 cells. Mice fed 0.5% cholic acid in normal chow showed an increase in endogenous SHP protein levels during both 12 hr and 24 hr treatment periods as compared to control mice fed only normal chow. In cultured HepG2 cells, treatment with CDCA did not noticeably change the rate of degradation in the endogenous SHP protein from cells not treated with CDCA. Although consistent with the previous studies on the exogenous ad-flag-SHP protein, treatment with FGF-19 significantly decreased the degradation rate of the endogenous SHP protein when HepG2 cells were treated with cyclohexamide. These results suggest that both bile acids and FGF-19 increase the endogenous SHP protein levels in mouse liver and HepG2 cells.

• Korean Journal of Veterinary Research
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• v.20 no.2
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• pp.167-173
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• 1980

The mean values of total protein, albumin, globulins and A/G ratio of synovial fluid from the normal tibiotarsal joints of 55 healthy Korean native cattle were investigated. The results obtained were summarized as followings. 1. The mean values of synovial total protein for the entire group were $0.98{\pm}0.05g/dl$, with a range of 0.43 to 1.83g/dl for individual samples, and $1.00{\pm}0.07g/dl$ in slaughtering cattle and $0.92{\pm}0.06g/dl$ in living group, respectively. Compared with serum, synovial fluid contained far less total protein(p<0.01). 2. The mean values for the group were; albumin, $0.42{\pm}0.02g/dl$, globulins, $0.56{\pm}0.04g/dl$, and A/G ratio, $0.99{\pm}0.10$, with a range of 0.17-0.82g/dl, 0.03-1.32g/dl, and 0.15-3.15 for individual sample, respectively. 3. No statistical significant differences in the mean values of total protein, albumin, globulins, and A/G ratio have been observed between the synovial fluids of slaughtering and living animals. 4. Significant correlations existed between the globulin levels of synovial fluid and serum(r=0.3939), but the other values were not established.

• Journal of Life Science
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• v.20 no.8
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• pp.1166-1172
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• 2010

Kinesin-I exists as a tetramer of two heavy chains (KHCs, also called KIF5s), which contain the amino (N)-terminal motor domain and carboxyl (C)-terminal domain, as well as two light chains (KLCs), which bind to the KIF5s (KIF5A, KIF5B and KIF5C) stalk region. To identify the interaction proteins for KIF5A, yeast two-hybrid screening was performed and a specific interaction with the ${\beta}$ subunit of heterotrimeric G proteins ($G{\beta}$) was found. $G{\beta}$ bound to the amino acid residues between 808 and 935 of KIF5A and to other KIF5 members in the yeast two-hybrid assay. The WD40 repeat motif of $G{\beta}$ was essential for interaction with KIF5A. In addition, these proteins showed specific interactions in the glutathione S-transferase (GST) pull-down assay. An antibody to KIF5s specifically co-immunoprecipitated KIF5s associated with heterotrimeric G proteins from mouse brain extracts. These results suggest that kinesin-I motor protein transports heteroterimeric G protein attachment vesicles along microtubules in the cell.

• Archives of Pharmacal Research
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• v.16 no.2
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• pp.114-117
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• 1993

Ginsenosides present in the roots of panax ginseng C.A. Meyer were shown to induce a stimulatory effect on the overexpressed cellular chicken c-src protein tyrossine kinase in NH3T3 cells. Among 4 ginsenosides studied $(G-Rb_2,\;G-Rc,\;G-Re\;and\;G-Rg_1),\;G-Rg_1$ showed the most stimulatory effect at $16.7\mu{g/ml}$ ginsenoside concentration increasing the activity by 2-4 times. Inhibitors of either protein synthesis or RNA synthesis blocked the activation of c-src proein tyrosine kinase. These results suggest that the csrc kinase activation apprars to involve an increase in the amount of protein of the kinase by transcriptional control mechanism rather than an increase in the kinase activity.

• BMB Reports
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• v.52 no.6
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• pp.397-402
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• 2019

Middle East respiratory syndrome coronavirus (MERS-CoV) uses the spike (S) glycoprotein to recognize and enter target cells. In this study, we selected two epitope peptide sequences within the receptor binding domain (RBD) of the MERS-CoV S protein. We used a complex consisting of the epitope peptide of the MERS-CoV S protein and CpG-DNA encapsulated in liposome complex to immunize mice, and produced the monoclonal antibodies 506-2G10G5 and 492-1G10E4E2. The western blotting data showed that both monoclonal antibodies detected the S protein and immunoprecipitated the native form of the S protein. Indirect immunofluorescence and confocal analysis suggested strong reactivity of the antibodies towards the S protein of MERS-CoV virus infected Vero cells. Furthermore, the 506-2G10G5 monoclonal antibody significantly reduced plaque formation in MERS-CoV infected Vero cells compared to normal mouse IgG and 492-1G10E4E2. Thus, we successfully produced a monoclonal antibody directed against the RBD domain of the S protein which could be used in the development of diagnostics and therapeutic applications in the future.