• Journal of the Korean Society of Food Science and Nutrition
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• v.39 no.10
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• pp.1481-1486
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• 2010

In this study we investigated the antioxidant activities and quality characteristics of Halocynthia aurantium and Halocynthia roretzi. The pH of H. aurantium was higher than that of H. roretzi. The volatile basic nitrogens of H. roretzi and H. aurantium were 22.41 mg% and 16.80 mg%, respectively. Lightness and yellowness of H. roretzi were higher than those of H. aurantium, but redness of H. aurantium was higher. The results of sensory evaluation showed that the H. aurantium was better for color, odor, taste and acceptability. Total combined amino acid contents of H. roretzi and H. aurantium were $36368.23\;{\mu}mol/g$ and $36500.12\;{\mu}mol/g$, respectively. Our results showed that H. roretzi had relatively higher contents of Asp, Glu, Gly, DPPH radical scavenging activity, ABTS radical scavenging activity and reducing power. Also total phenol content of H. roretzi was higher than that of H. aurantium. The organoleptic properties of the H. aurantium were superior but the antioxidant activities were relatively lower than those of H. aurantium. For commercial usage, additional study would be helpful in the two ascidians to recommend.

• Journal of Life Science
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• v.7 no.4
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• pp.392-401
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• 1997

The poliovirus is a small, and non-enveloped virus. The RNA genome of poliovirus is continuous, linear, and has a single open reading frame. This polyprotein precursor is cleaved proteolytically to yield mature products. Most of the cleavages occur by viral protease. The mature proteins derived from the P1 polyprotein precursor are the structural components of the viral capsid. The initial cleavage by 2A protease is indirectly involved in the cleavage of a cellular protein p220, a subunit of the eukaryotic translation initiation factor 4F. This cleavage leads to the shut-off of cap-dependent host cell translation, and allows poliovirus to utilize the host cell machinery exclusively for translation its own RNA, which is initiated by internal ribosome entry via a cap-independent mechanism. The functional role of the 2B, 2C and 2BC proteins are not much known. 2B, 2C, 2BC and 3CD proteins are involved in the replication complex of virus induced vesicles. All newly synthesized viral RNAs are linked with VPg. VPg is a 22 amino acid polypeptide which is derived from 3AB. The 3C and 3CD are protease and process most of the cleavage sites of the polyprotein precursor. The 3C protein is also involved in inhibition of RNA polymerase II and III mediated transcription by converting host transcription factor to an inactive form. The 3D is the RNA dependent RNA polymerase. It is known that poliovirus replication follows the general pattern of positive strand RNA virus. Plus strand RNA is transcribed into complementary minus strand RNA that, in turn, is transcribed for the synthesis of plus strand RNA is transcribed into complementary minus strand RNA that, in turn, is transcribed for the synthesis of plus strand RNA strands. Poliovirus RNA synthesis occurs in a membranous environment but how the template RNA and proteins required for RNA replication assemble in the membrane is not much known. The RNA requirements for the encapsidation of the poliovirus genome (packaging signal) are totally unknown. The poliovirus infection cycle lasts approximately 6 hours.

• Journal of agriculture & life science
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• v.43 no.6
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• pp.85-93
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• 2009

The boiled oyster vacuum-packed in cylindrical can(No. 301-3) were thermally processed at $115^{\circ}C$ to reach Fo values of 5~20 min. The yield was slightly decreased with the increasing of Fo-values (79.2~ 83.7%), and volatile basic nitrogen (VBN) contents increased markedly with the increasing of Fo-value. In fatty acid composition of canned oyster, the composition ratio of saturates and monoenes such as 14:0, 16:0 and 18:1n9 increased, while polyunsaturated fatty acids such as 20:5n-3 and 22:6n-3 decreased with the increasing of Fo-value. In taste compounds, content of total free amino acid in raw oyster was 1,533.5 mg%, and this total content was slightly increased (1,140.8~1,266.2 mg%) with the increasing of Fo values. But contents of betaine and ionic minerals such as Na, K, Mg and P decreased markedly by thermal processing at $115^{\circ}C$. As compared with Fo 5 min. heat treatment; Fo 20 min. heat treatment at $115^{\circ}C$ became more hardened in texture of oyster meat. In sensory evaluations on organoleptic characteristics, no significant difference at 5% level was observed among the canned boiled oyster meats heated at Fo 5~15 min.

• Journal of Life Science
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• v.33 no.11
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• pp.868-875
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• 2023

Kinesin-1 is a motor protein identified as the first member of the kinesin superfamily (KIF), which plays a role in intracellular cargo transport by acting as microtubule-dependent motor proteins within cells. Kinesin-1 consists of two heavy chains (KHCs, also known as KIF5s) and two light chains (KLCs). The 93 amino acids in the carboxyl (C)-terminal tail region of KIF5A are not homologous to the C-terminal tail region of KIF5B or the C-terminal tail region of KIF5C. In this study, we used a yeast two-hybrid screen to identify the binding proteins that interacted with the C-terminal region of KIF5A. We found an association between KIF5A and CUE domain containing 2 (CUEDC2), which is proposed to function as an adaptor protein involved in ubiquitination pathways and protein trafficking. CUEDC2 bound to the C-terminal region of KIF5A and did not interact with KIF5B (the motor of kinesin-1), KIF3A (the motor of kinesin-2), or kinesin light chain 1 (KLC1). KIF5A specifically bound to the C-terminal region of CUEDC2. Furthermore, KIF5A did not interact with another isoform: CUEDC1. In addition, glutathione S-transferase (GST) pull-downs showed that KIF5A directly bound GST-CUEDC2 but did not interact with GST-CUEDC1 and GST alone. When myc-KIF5A and EGFP-CUEDC2 were co-expressed in HEK-293T cells, CUEDC2 co-immunoprecipitated with kinesin-1, and myc-KIF5A and FLAG-CUEDC2 colocalized in the cells. These results suggest that in intracellular cargo transport by kinesin-1, CUEDC2 serves as an adaptor protein connecting kinesin-1 and cargo by binding to KIF5A.

• Journal of Life Science
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• v.34 no.5
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• pp.333-338
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• 2024

Kinesin-1 is a heterotetrameric protein composed of two heavy chains (KHCs, also known as KIF5s) with a motor domain and two light chains (KLCs) without a motor domain. KIF5 has three subtypes, namely, KIF5A, KIF5B, and KIF5C, which share high amino acid homology except in their carboxy (C)-terminal region. KIF5A is responsible for transporting cargo within the cell. The adaptor proteins that bind to the C-terminal region of KIF5A mediate between kinesin-1 and cargo. However, the proteins regulating the intracellular cargo transport of kinesin-1 have not yet been fully identified. In this study, we identified ADP-ribosylation factor GTPase-activating protein 1 (ArfGAP1), which is involved in the intracellular trafficking of lysosomes, as a binding partner of KIF5A. KIF5A binds to the C-terminal region of ArfGAP1, and ArfGAP1 binds to the C-terminal region of KIF5A but does not interact with KIF5B, KIF5C, kinesin light chain 1 (KLC1), or KIF3A. When co-expressed in mammalian cells, ArfGAP1 co-localized with KIF5A and co-immunoprecipitated with KIF5A, KIF5B, and KLC1, but not with KIF3B. These results suggest that kinesin-1 may be regulated by ArfGAP1 in the intracellular transport of cargo.