• Title/Summary/Keyword: Fish protein

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Toxic Effects on the Nonspecific Immune System of the Rock Bream Oplegnathus fasciatus upon Exposure to Di-2-ethylhexyl Phthalate

  • Kim, Jun-Hwan;Jeong, Dal-Sang;Kang, Ju-Chan
    • Fisheries and Aquatic Sciences
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    • v.16 no.3
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    • pp.171-176
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    • 2013
  • The aim of this study was to investigate the in vivo toxicity of di-2-ethylhexyl phthalate (DEHP), on the immune system of the rock bream, Oplegnathus fasciatus. Fish were injected twice intraperitoneally with DEHP (200, 400, and 800 mg/kg BW), and the cellularity and functional activity of phagocytes in the spleen and head kidney were measured. The number of head kidney leukocyte cells was significantly greater in fish treated with 800-mg DEHP/kg BW. Nonspecific immunity, as determined by the phagocytic index, was significantly decreased at 800-mg DEHP/kg BW in the head kidney. A significant reduction in phagocytic capacity was observed in the head kidney at ${\geq}$400-mg DEHP/kg BW. Furthermore, significantly increased levels of serum glutamic oxaloacetate transaminase and glutamic pyruvate transaminase indicated a marked hepatic dysfunction in immunosuppressed fish. Total serum protein was significantly reduced at ${\geq}$400-mg DEHP/kg BW; however, there were no significant changes in lysozyme activity. These results demonstrate that immune responses in the rock bream, Oplegnathus fasciatus can predict immunotoxicity at doses ${\geq}$400-mg DEHP/kg BW.

Genomic DNA Sequence of Mackerel Parvalbumin and a PCR Test for Rapid Detection of Allergenic Mackerel Ingredients in Food

  • Choi, Ka-Young;Hong, Kwang-Won
    • Food Science and Biotechnology
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    • v.16 no.1
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    • pp.67-70
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    • 2007
  • Mackerel (Scomber japonicus) often causes severe allergic reactions in sensitive people. Food containing undeclared mackerel may pose a risk to such people. The major allergenic protein in fish such as mackerel, codfish, and Alaska pollack has been found to be parvalbumin. In this study, we developed a polymerase chain reaction (PCR) method to detect mackerel DNA using primers corresponding to the parvalbumin gene. We cloned and sequenced 1.5 kb of parvalbumin gene by PCR using mackerel genomic DNA as a template. Nucleotide sequence analysis of genomic parvalbumin gene, composed of 4 exons and 3 introns, allowed the selection of two pairs of oligonucleotide primers specific for mackerel. These primers successfully enabled PCR amplification of specific regions of genomic parvalbumin DNA from mackerel, but no amplification from 8 other fish samples, surimi, and 6 boiled fish pastes. The sensitivity of this method was sufficient to detect 5 ng of purified mackerel DNA mixed with 50 ng of surimi DNA. This rapid and specific method for the detection of allergenic mackerel would be beneficial in reducing food allergy caused by the ingestion of hidden allergen in processed food.

Molecular cloning and expression analysis of a ferritin H subunit from rock bream, Oplegnathus fasciatus (돌돔 ferritin H 유전자의 클로닝과 발현 분석)

  • Kwon, Mun-Gyeong;Jeong, Ji-Min;Kim, Ju-Won;Park, Chan-Il
    • Journal of fish pathology
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    • v.26 no.3
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    • pp.295-301
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    • 2013
  • Ferritin is an evolutionarily conserved protein that plays an important role in iron storage and detoxification. In this study, the gene encoding a ferritin H subunit homologue (RbFH) was cloned from rock bream (Oplegnathus fasciatus) and analyzed at the expression. The full-length ferritin H cDNA was 1162 bp long and contained an open reading frame (ORF) of 531 bp that encoded 177 amino acid residues with a predicted molecular mass of 20.8 kDa. The 5' UTR was 297 bp in length, and the 3' UTR 298 bp, and preceded by a 5'-untranslated region that contains a putative Iron Regulatory Element (IRE). The deduced amino acid sequence of RbFH shares extensive sequence identities with the H ferritins of a number of fish species and contains the ferroxidase center that is preserved in ferritin H subunits. Examination of tissue specific expression indicated that RbFH expression was most abundant in PBLs, RBC, liver and muscle.

Production of monoclonal antibodies against marine birnavirus (Marine birnavirus (MABV)에 대한 단클론 항체 생산)

  • Kong, Kyoung-Hui;Oh, Myung-Joo;Kim, Wi-Sik
    • Journal of fish pathology
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    • v.33 no.2
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    • pp.171-175
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    • 2020
  • We developed and subsequently characterized mouse monoclonal antibodies (mAbs) against marine birnavirus (MABV). Eight hybridoma clones secreting mAbs against MABV were established. All eight mAbs (8G6, 11C3, 15E3, 17H6, 32A6, 35A7, 38B5, and 47E3) were reacted with viral protein 3 of MABV in MABV-infected CHSE-214, whereas, no reactivity was observed in normal CHSE-214 by western blot analysis. Moreover, these eight mAbs were strongly reacted with MABV, and no cross-reactivity has been observed against other five fish viruses (hirame rhabdovirus, infectious hematopoietic necrosis virus, nervous necrosis virus, spring viraemia of carp virus, and viral hemorrhagic septicemia virus), although five mAb (11C3, 15E3, 17H6, 32A6, and 38B5) reacted with both MABV and infectious pancreatic necrosis virus by enzyme linked immunosorbent assay (ELISA). These results indicate that the mAbs can be of value in MABV detection.

Activating and inactivating mutations of the human, rat, equine and eel luteinizing hormone/chorionic gonadotropin receptors (LH/CGRs)

  • Min, Kwan-Sik;Byambaragchaa, Munkhzaya;Choi, Seung-Hee;Joo, Hyo-Eun;Kim, Sang-Gwon;Kim, Yean-Ji;Park, Gyeong-Eun
    • Journal of Animal Reproduction and Biotechnology
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    • v.36 no.4
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    • pp.169-174
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    • 2021
  • Mutations in the luteinizing hormone/chorionic gonadotropin receptors (LH/CGRs), representatives of the G protein-coupled receptor family, have been rapidly identified over the last 20 years. This review aims to compare and analyze the data reported the activating and inactivating mutations of the LH/CGRs between human, rat, equine and fish, specifically (Japanese eel Anguilla japonica). Insights obtained through detailed study of these naturally-occurring mutations provide a further update of structure-function relationship of these receptors. Specifically, we present a variety of data on eel LH/CGR. These results provide important information about LH/CGR function in fish and the regulation of mutations of the highly conserved amino acids in glycoprotein hormone receptors.

Cross-Linked Collagen Scaffold from Fish Skin as an Ideal Biopolymer for Tissue Engineering

  • Biazar, Esmaeil;Kamalvand, Mahshad;Keshel, Saeed Heidari;Pourjabbar, Bahareh;Rezaei-Tavirani, Mustafa
    • Korean Journal of Materials Research
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    • v.32 no.4
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    • pp.186-192
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    • 2022
  • Collagen is one of the most widely used biological materials in medical design. Collagen extracted from marine organisms can be a good biomaterial for tissue engineering applications due to its suitable properties. In this study, collagen is extracted from fish skin of Ctenopharyngodon Idella; then, the freeze drying method is used to design a porous scaffold. The scaffolds are modified with the chemical crosslinker N-(3-Dimethylaminopropyl)-N'-ethyl carbodiimide hydrochloride (EDC) to improve some of the overall properties. The extracted collagen samples are evaluated by various analyzes including cytotoxicity test, SDS-PAGE, FTIR, DSC, SEM, biodegradability and cell culture. The results of the SDS-PAGE study demonstrate well the protein patterns of the extracted collagen. The results show that cross-linking of collagen scaffold increases denaturation temperature and degradation time. The results of cytotoxicity show that the modified scaffolds have no toxicity. The cell adhesion study also shows that epithelial cells adhere well to the scaffold. Therefore, this method of chemical modification of collagen scaffold can improve the physical and biological properties. Overall, the modified collagen scaffold can be a promising candidate for tissue engineering applications.

Reference intervals of hematological and histopathological index at three different temperatures in Korean rockfish Sebastes schlegelii (조피볼락의 수온별 혈액학적 및 병리조직학적 정상치 탐색)

  • Beom Hee Lee;Sang Bin Lee;Eul Bit Noh;Ji Min Ryu;Bo Seong Kim
    • Journal of fish pathology
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    • v.36 no.2
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    • pp.369-378
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    • 2023
  • In this study, clinically healthy Korean rockfish were provided by a farm and then raised in a lab for 14 days at three different temperatures (10℃, 15℃, and 20℃) to establish hematological, blood biochemical, and histopathological reference intervals against normal fish. Hematocrit, MCV, MCHC, total protein, BUN, and GPT values in the blood showed significant differences among temperature groups. As the water temperature increased, neutrophil, thrombocyte, and lymphocyte counts also rose, while the monocyte value peaked at 15℃. The histopathological score revealed significant variations in the gills, stomach, and inflammation indices by temperature group; the gills and inflammation indices peaked at 20℃, whereas the stomach index peaked at 15℃. It is expected that information on these normal values will serve as a fundamental collection of data for further studies related to laboratory-based experiments.

Production of monoclonal antibodies against infectious hematopoietic necrosis virus (IHNV) (Infectious hematopoietic necrosis virus (IHNV)에 대한 단클론 항체 생산)

  • Kyoung-Hui Kong;Myung-Joo Oh;Choon-Sup Kim;Wi-Sik Kim
    • Journal of fish pathology
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    • v.36 no.2
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    • pp.389-394
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    • 2023
  • Infectious hematopoietic necrosis virus (IHNV) is s significant viral pathogen affecting cultured rainbow trout (Oncorhynchus mykiss) in Korea. In this study, five monoclonal antibodies (mAbs) (IHNV-1, 2, 3, 4, and 5) were produced using purified IHNV. Reactivities of these mAbs were analyzed by western blot (WB), enzyme-linked immunosorbent assay (ELISA), and indirect fluorescent antibody test (IFAT). These mAbs recognized glycoprotein (69 kDa, IHNV-1), nucleocapsid protein (39 kDa, IHNV-3, 4, and 5), or phosphoprotein (27 kDa, IHNV-2) of IHNV by WB analysis. ELISA results indicated that these five mAbs were specific to IHNV without showing any cross-reactivity against other fish viruses (hirame rhabdovirus, infectious pancreatic necrosis virus, and viral hemorrhagic septicemia virus). IFAT demonstrated specific fluorescence signals of IHNV-infected epithelioma papulosum cyprini (EPC) cells, whereas no reactivity of normal EPC cells was observed. These mAbs can be very useful for immuno-diagnosis of IHNV infection.

Biochemical Composition of Rotifer, Brachionus plicatilis Enriched with Different Commercial Enrichments (영양 강화제 종류에 따른 rotifer, Brachionus plicatilis의 생화학적 조성)

  • ;Joseph A. Brown
    • Journal of Aquaculture
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    • v.17 no.3
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    • pp.187-196
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    • 2004
  • This study was carried out to investigate changes in biochemical composition of rotifer, Brachionus plicatilis, enriched with the commercial enrichments (Enhance, Advantage, Algamac-2000, DHA-Selco and Advantage + Chlorella) at various durations of enrichment (0, 6, 12 and 24 hr) to improve the growth and survival of marine fish larvae. Total lipid content of rotifers enriched with various enrichments tended to increase with an increase in durations of enrichment up to 6 hr, but after that, was not significantly affected by enrichment materials. However, total protein content of rotifers enriched groups except for Advantage+Chlorella decreased with the increase in duration of enrichment. The highest protein/lipid ratio showed 2.7 in rotifer enriched with the Advantage +Chlorella. The phospholipid/lipid ratio of rotifer enriched with the Enhance, Advantage and Advantage+Chlorella groups was significantly higher than that of enriched rotifer with the Algamac-2000 and DHA-Selco groups. The highest DHA level, 2.5%, of rotifer enriched for 24 hr was obtained in the Advantage, but was not significantly different among other groups, except for Algamac-2000. No significant difference in DHA level of rotifer enriched with the DHA-Selco, Algamac-2000 and Advantage+Chlorella groups was observed between l2h and 24hr of enrichment. The DHA/EPA ratio in the enriched rotifers varied among enrichment material groups, ranged from a high level of 11.1:1 in the Advantage+Chlorella group to a low level of 4.1:1 in DHA-Selco group. The results from this study indicate that rotifers enriched with Enhance, Advantage and Advantage+Chlorella seemed to be effective to improve nutritional value of rotifer for marine fish larvae because phospholipid, DHAJEPA and protein/lipid ratios of rotifer enriched with Enhance, Advantage+Chlorella were higher than those of rotifer enriched with either DHA-Selco or Algamac-2000. Especially, supplementation of the Chlorella to these enrichments would appear to be effective for improvement of fish larval performance because of no reduction of protein level in rotifer, which is critical for growth of fish larvae.

Interaction of Porcine Myofibrillar Proteins and Various Gelatins: Impacts on Gel Properties

  • Noh, Sin-Woo;Song, Dong-Heon;Ham, Youn-Kyung;Kim, Tae-Kyung;Choi, Yun-Sang;Kim, Hyun-Wook
    • Food Science of Animal Resources
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    • v.39 no.2
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    • pp.229-239
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    • 2019
  • The objectives of this study were to determine the interaction between porcine myofibrillar proteins and various gelatins (bovine hide, porcine skin, fish skin, and duck skin gelatins) and their impacts on gel properties of porcine myofibrillar proteins. Porcine myofibrillar protein was isolated from pork loin muscle (M. longissimus dorsi thoracis et lumborum). Control was prepared with only myofibrillar protein (60 mg/mL), and gelatin treatments were formulated with myofibrillar protein and each gelatin (9:1) at the same protein concentration. The myofibrillar protein-gelatin mixtures were heated from $10^{\circ}C$ to $75^{\circ}C$ ($2^{\circ}C/min$). Little to no impacts of gelatin addition on pH value and color characteristics of heat-induced myofibrillar protein gels were observed (p>0.05). The addition of gelatin slightly decreased cooking yield of heat-induced myofibrillar protein gels, but the gels showed lower centrifugal weight loss compared to control (p<0.05). The addition of gelatin significantly decreased hardness, cohesiveness, gumminess, and chewiness of heat-induced myofibrillar gels. Further, sodium dodecyl poly-acrylamide gel electrophoresis (SDS-PAGE) showed no interaction between myofibrillar proteins and gelatin under non-thermal conditions. Only a slight change in the endothermic peak (probably myosin) of myofibrillar protein-gelatin mixtures was found. The results of this study show that the addition of gelatin attenuated the water-holding capacity and textural properties of heat-induced myofibrillar protein gel. Thus, it could be suggested that well-known positive impacts of gelatin on quality characteristics of processed meat products may be largely affected by the functional properties of gelatin per se, rather than its interaction with myofibrillar proteins.