• Proceedings of the Zoological Society Korea Conference
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• 1995.10b
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• pp.330.2-330
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• 1995

No Abstract, See Full Text

• Bulletin of the Korean Chemical Society
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• v.18 no.7
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• pp.687-689
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• 1997

• Asian-Australasian Journal of Animal Sciences
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• v.14 no.7
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• pp.1008-1013
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• 2001

This experiment was conducted to determine the effects of enzyme supplementation on the performance of 80 growing-finishing pigs (26.2 kg) fed diets containing either soybean or canola meal. Barley-based diets formulated using either soybean meal or canola meal were fed with or without enzyme (Allzyme Vegpro, Alltech Biotechnology Centre). Eight castrates and twelve gilts were fed each diet. Digestibility of dry matter, crude protein and gross energy was 8.0 (p=0.0001), 7.9 (p=0.0005) and 7.9 (p=0.0003) percent lower for pigs fed diets containing canola meal compared with soybean meal. Enzyme supplementation had no effect on nutrient digestibility (p>0.05). There was a significant interaction between protein source and enzyme for all three nutrients. Over the entire experimental period (26.2 to 77.9 kg), pigs fed canola meal consumed 9.4% less feed (p=0.001), gained weight 20.4% slower (p=0.001) and had a 12.9% poorer feed conversion (p=0.001) than pigs fed soybean meal. Weight gain, feed intake and feed conversion were unaffected by enzyme addition (p>0.05). Castrates gained weight 11.4% faster (p=0.001), consumed 9.3% more feed (p=0.001) and had a 2.6% better feed conversion (p=0.026) than gilts. There was a significant interaction between protein source and sex of pig for feed conversion. Pigs fed diets based on canola meal had a significantly lower carcass value index (p=0.01), lower lean yield (p=0.007) and lower lean depth over the loin (p=0.001) than pigs fed diets based on soybean meal. Enzyme addition significantly increased lean depth over the loin (p=0.01). There was a significant interaction between protein source and enzyme for carcass value index (p=0.04), estimated lean yield (p=0.05) and fat depth over the loin (p=0.05). These results confirm previous studies which have demonstrated poorer pig performance when canola meal completely replaces soybean meal in diets fed to growing-finishing pigs. In addition, the results provide little justification for the inclusion of the Vegpro enzyme in diets fed to pigs of this weight range.

• Journal of the Korean Vacuum Society
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• v.16 no.1
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• pp.52-57
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• 2007

The interaction force between biomolecules(DNA-DNA, antigen-antibody, ligand-receptor, protein-protein) defines not only biomolecular function, but also their mechanical properties and hence bio-sensor. Atomic force microscopy(AFM) is nowadays frequently applied to determine interaction forces between biological molecules and biomolecular force measurements, obtained for example using AFM can provide valuable molecular-level information on the interactions between biomolecules. A proper modification of an AFM tip and/or a substrate with biomolecules permits the direct measurement of intermolecular interactions, such as DNA-DNA, protein-protein, and ligand-receptor, etc. and a microcantilever-based sensor appeared as a promising approach for ultra sensitive detection of biomolecular interactions.

• BMB Reports
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• v.44 no.9
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• pp.572-577
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• 2011

Elevated phospholipase D (PLD) expression prevents cell cycle arrest and apoptosis. However, the roles of PLD isoforms in cell proliferation and apoptosis are incompletely understood. Here, we investigated the physiological significance of the interaction between PLD2 and protein kinase CKII (CKII) in HCT116 human colorectal carcinoma cells. PLD2 interacted with the CKII${\beta}$ subunit in HCT116 cells. The C-terminal domain (residues 578-933) of PLD2 and the N-terminal domain of CKII${\beta}$ were necessary for interaction between the two proteins. PLD2 relocalized CKII${\beta}$ to the plasma membrane area. Overexpression of PLD2 reduced CKII${\beta}$ protein level, whereas knockdown of PLD2 led to an increase in CKII${\beta}$ expression. PLD2-induced CKII${\beta}$ reduction was mediated by ubiquitin-dependent degradation. The C-terminal domain of PLD2 was sufficient for CKII${\beta}$ degradation as the catalytic activity of PLD2 was not required. Taken together, the results indicate that the C-terminal domain of PLD2 can regulate CKII by accelerating CKII${\beta}$ degradation in HCT116 cells.

• Parasites, Hosts and Diseases
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• v.46 no.4
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• pp.209-216
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• 2008

A monoclonal antibody against Toxoplasma gondii of Tg556 clone (Tg556) blotted a 29 kDa protein, which was localized in the dense granules of tachyzoites and secreted into the parasitophorous vacuolar membrane (PVM) after infection to host cells. A cDNA fragment encoding the protein was obtained by screening a T. gondii cDNA expression library with Tg556, and the full-length was completed by 5'-RACE of 2,086 bp containing an open reading frame (ORF) of 669 bp. The ORF encoded a polypeptide of 222 amino acids homologous to the revised GRA3 but not to the first reported one. The polypeptide has 3 hydrophobic moieties of an N-terminal stop transfer sequence and 2 transmembrane domains (TMD) in posterior half of the sequence, a cytoplasmic localization motif after the second TMD and an endoplasmic reticulum (ER) retrival motif in the C-terminal end, which suggests GRA3 as a type III transmembrane protein. With the ORF of GRA3, yeast two-hybrid assay was performed in HeLa cDNA expression library, which resulted in the interaction of GRA3 with calcium modulating ligand (CAMLG), a type II transmembrane protein of ER. The specific binding of GRA3 and CAMLG was confirmed by glutathione S-transferase (GST) pull-down and immunoprecipitation assays. The localities of fluorescence transfectionally expressed from GRA3 and CAMLG plasmids were overlapped completely in HeLa cell cytoplasm. In immunofluorescence assay, GRA3 and CAMLG were shown to be co-localized in the PVM of host cells. Structural binding of PVM-inserted GRA3 to CAMLG of ER suggested the receptor-ligand of ER recruitment to PVM during the parasitism of T. gondii.

• BMB Reports
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• v.41 no.7
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• pp.511-515
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• 2008

The nucleocapsid (NC) protein of the Human Immunodeficiency Virus-1 plays a key role in viral genomic packaging by specifically recognizing the Psi($\Psi$) RNA sequence within the HIV-1 genome RNA. Recently, a novel cell-based assay was developed to probe the specific interactions in vivo between the NC and $\Psi$-RNA using E.coli cells (J. Virol. 81: 6151-55, 2007). In order to examine the extendibility of this cell-based assay to RNAs other than $\Psi$-RNA, this study tested the RNA aptamers isolated in vitro using the SELEX method, but whose specific binding ability to NC in a living cellular environment has not been established. The results demonstrate for the first time that each of those aptamer RNAs can bind specifically to NC in a NC zinc finger motif dependent manner within the cell. This confirms that the cell-based assay developed for NC-$\Psi$interaction can be further extended and applied to NC-binding RNAs other than $\Psi$-RNA.

• Journal of Life Science
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• v.19 no.7
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• pp.859-865
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• 2009

Microtubules, a major cytoskeleton, form parallel arrays in the axon and are oriented with their plus ends toward the cell periphery. Kinesin superfamily proteins (KIFs) are the molecular motors acting in the microtubule-based motilities of organelles in cells. Here, we used the yeast two-hybrid system to identify the protein that interacts with the coiled-coil domain of KIF1A and found a specific interaction with microtubule-destabilizing factor SCG10. SCG10 bound to the amino acid residues between 400 and 820 of KIF1A, but not to other KIFs in the yeast two-hybrid assay. The coiled-coil domain of SCG10 is essential for interaction with KIF1A. In addition, this specific interaction was also observed in the Glutathione S-transferase pull-down assay. An antibody to SCG10 specifically co-immunoprecipitated KIF1A associated with SCG10 from mouse brain extracts. These results suggest that KIF1A motor protein transports SCG10-containing vesicles along microtubules in neurons.

• Genomics & Informatics
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• v.21 no.2
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• pp.23.1-23.9
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• 2023

The mammalian sirtuin family, consisting of SIRT1-SIRT7, plays a vital role in various biological processes, including cancer, diabetes, neurodegeneration, cardiovascular disease, cellular metabolism, and cellular homeostasis maintenance. Due to their involvement in these biological processes, modulating sirtuin activity seems promising to impact immuneand aging-related diseases, as well as cancer pathways. However, more understanding is required regarding the safety and efficacy of sirtuin-targeted therapies due to the complex regulatory mechanisms that govern their activity, particularly in the context of multiple targets. In this study, the interaction landscape of the sirtuin family was analyzed using a systems biology approach. A sirtuin protein-protein interaction network was built using the Cytoscape platform and analyzed using the NetworkAnalyzer and stringApp plugins. The result revealed the sirtuin family's association with numerous proteins that play diverse roles, suggesting a complex interplay between sirtuins and other proteins. Based on network topological and functional analysis, SIRT1 was identified as the most prominent among sirtuin family members, demonstrating that 25 of its protein partners are involved in cancer, 22 in innate immune response, and 29 in aging, with some being linked to a combination of two or more pathways. This study lays the foundation for the development of novel therapies that can target sirtuins with precision and efficacy. By illustrating the various interactions among the proteins in the sirtuin family, we have revealed the multifaceted roles of SIRT1 and provided a framework for their possible roles to be precisely understood, manipulated, and translated into therapeutics in the future.

• Journal of Sensor Science and Technology
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• v.20 no.4
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• pp.226-229
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• 2011

Label-free detection of biomolecular interactions was performed using BioFET(Biologically sensitive Field-Effect Transistor) and SPR(Surface Plasmon Resonance). Qualitative information on the immobilization of an anti-IgG and antibody-antigen interaction was gained using the SPR analysis system. The BioFET was used to explore the pI value of the protein and to monitor biomolecular interactions which caused an effective charge change at the gate surface resulting in a drain current change. The results show that the BioFET can be a useful monitoring tool for biomolecular interactions and is complimentary to the SPR system.