• Title/Summary/Keyword: heavy chain

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Endoplnsmic Reticulum Stress Up-regulates Ferritin Heavy Chain 1 Expression

  • Jin, Cho-Yi;Kwon, Ki-Sang;Yun, Eun-Young;Goo, Tae-Won;Kwon, O-Yu
    • Biomedical Science Letters
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    • v.13 no.2
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    • pp.153-155
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    • 2007
  • Ferritin heavy chain 1 (FTH1) is an ubiquitous and highly conserved protein which plays a major role in iron homeostasis. The expression of FTH1 was specifically enhanced under various condition of endoplasmic reticulum (ER) stresses drugs such as Brefeldin A (BFA), DTT (Dithiothreitol), calcium ionophore A23187 and tunicamycin. We firstly report here that ER-stress induces up-regulated expression of FTH1 in FRTL-5 culture thyrocytes.

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Study on Multibody Dynamic Analysis and Durability of Heavy Load Bucket Roller Chain System (고하중용 버킷 롤러체인 시스템의 다물체 동역학 해석 및 내구성 연구)

  • Kim, Chang Uk;Park, Jin Chul;Lee, Dong Woo;Song, Jung Il
    • Journal of the Korean Society for Precision Engineering
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    • v.33 no.11
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    • pp.919-925
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    • 2016
  • In this study, multibody dynamic and mechanical analyses were conducted for the structure of roller chain bucket elevator system. The fatigue life of the roller chain elevator system was determined under static and fatigue loadings. Results of multibody dynamic analysis suggested that the maximum contact force occurred at the drive sprocket engagement point with the roller chain due to maximum tension. Fatigue analysis results suggest that the high load roller chain system is durable and safe because its life time is more than 700,000 cycles, close to its designed value (1,000,000 cycle). However, the contact portion of plate and pin needed a safety factor. The dynamic analysis of the heavy load roller chain was conducted with a multibody dynamic analysis program. The results obtained in this study can be utilized for dynamic analysis of roller chain systems in all industries.

Forecasting Modeling of Heavy Tail Typed Demand using Student's t-Copula Fitting in Supply Chain Management (Student's t-Copula 적합을 통한 Heavy Tail형 SCM 수요 데이터의 모델링 및 분석)

  • Kim, Taesung;Lee, Hyunsoo
    • Journal of Digital Convergence
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    • v.11 no.9
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    • pp.103-111
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    • 2013
  • As the demand-oriented management has been getting important in Supply Chain Management (SCM), various forecasting methods have been suggested including regression analyses. However, dependency structures among variables have been captured by a correlation coefficient, only. It results in inaccurate demand predictions. This paper suggests a new and effective forecasting modeling framework using student's t-copula function. In order to show overall modeling procedures framework, heavy tail typed numerical data and its copula estimations are provided. The suggested methodology can contribute to decrease the bullwhip effect and to stabilize volatile environment in a supply chain network.

Influences of Squid Ink Added to Low-Salted Squid Jeot-gal on Its Proteolytic Characteristics (오징어 먹즙 첨가가 저 식염 오징어 젓갈의 단백질분해 특성에 미치는 영향)

  • Oh, Sung-Cheon
    • Journal of the Korean Applied Science and Technology
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    • v.30 no.2
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    • pp.348-355
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    • 2013
  • Squid ink was added to the salt fermented squid by 2% or 4% of concentration and ripened at $10^{\circ}C$ for 8 weeks and at $20^{\circ}C$ for 32days. The effects of the squid ink on the amino nitrogen and muscle protein of salt fermented squid were investigated. The results are as follows; As the salt concentration was decreased and the fermentation temperature raised, amino nitrogen in the salt fermented squid without addition of the squid ink was significantly increased to the latter stage of the ripening and hence fermentations were enhanced. From the change of the protein in the squid muscle in the experiments, dissolution of the myosin heavy chain took place conspicuously in the early stage of the ripening while actin was rarely changed which resulted in the strong resistance to protease. The amino nitrogen content in the salt fermented squid addition of the squid ink has increased to the latter part of the ripening but the range was smaller than no treatment groups. The protein in squid muscle, especially the myosin heavy chain was remarkably dissolved in the middle of the ripening whereas the squid ink added groups of high salt concentration and low temperature showed the tendency of slow proteolysis.

Construction of cDNA Library from Posterior Silk Gland (PSG) of Korean Oak Silkmoth, Antheraea yamamai and Molecular Cloning of Fibroin Heavy Chain Gene(FHC)

  • Lee, Jin-Sung;Kim, Soon-Jung;Kim, Ki-Hwan;Park, Young-Min;Suh, Dong-Sang
    • Journal of Life Science
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    • v.10 no.1
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    • pp.10-13
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    • 2000
  • To develope the genetic source of oak wild silkworm, Antheraea yamamai, the cDNA library was constructed with poly A+ mRNA isolated from posterial silk gland of fifth instar larvae. Titer of the cDNA library was about 5.1$\times$105 pfu in total. We presumed that the titer covered almost all transcripts existed in Antherea yamamai. From cDNA library of Antheraea yamamai, fibroin heavy chain gene, which is specifically expressed from posterial silk gland of Antheraea yamamai, was screened using oligonuclotide probe specific to alanine rich motif of fibrin heavy chain gene of Antheraea pernyi. As a result, fibroin clones isolated from 5$\times$104 plaques showed the highest homolgy (95%) with that of Antherea pernyi in nucleotide of Anthereaea yamamai and Bombyx mori shows that there is no homologous sequence in the 3+ partial 채야후 region Genomic southern hybridization suggested that one copy is present. Northern hybridization showed that fibroin transcript was approximateely 9 kb in length.

Analysis of Myosin Heavy Chain Isoforms from Longissimus Thoracis Muscle of Hanwoo Steer by Electrophoresis and LC-MS/MS

  • Kim, Gap-Don
    • Food Science of Animal Resources
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    • v.34 no.5
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    • pp.656-664
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    • 2014
  • The purpose of this study was to analyze myosin heavy chain (MHC) isoforms in bovine longissimus thoracis (LT) muscle by liquid chromatography (LC) and mass spectrometry (MS). LT muscles taken from Hanwoo (Korean native cattle) steer (n=3) used to separate myosin bands by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The peptide queries were obtained from the myosin bands by LC-MS/MS analysis following in-gel digestion with trypsin. A total of 33 and 43 queries were identified as common and unique peptides, respectively, of MHC isoforms (individual ions scores >43 indicate identity or extensive homology, p<0.05). MHC-1 (IIx), -2 (IIa), -4 (IIb), and -7 (slow/I) were identified based on the Mowse score (5118, 3951, 2526, and 2541 for MHC-1, -2, -4, and -7, respectively). However, more analysis is needed to confirm the expression of MHC-4 in bovine LT muscle because any query identified as a unique peptide of MHC-4 was not found. The queries that were identified as unique peptides could be used as peptide markers to confirm MHC-1 (14 queries), -2 (8 queries), and -7 (21 queries) in bovine LT muscle; no query identified as a unique peptide of MHC-4 was found. LC-MS/MS analysis is a useful approach to study MHC isoforms at the protein level.

Effect of recombinant yeast producing Sus scrofa ferritin Heavy-chain on piglets (자돈에서 Sus scrofa ferritin Heavy-chain 생산 재조합 효모의 효과)

  • Choi, Young-Jun;Lim, Hwan;Kim, Hyeon-Cheol;Kim, Jong-Taek;Rhee, Ki-Jong;Jung, Bae-Dong
    • Korean Journal of Veterinary Service
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    • v.35 no.4
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    • pp.307-312
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    • 2012
  • Iron deficiency anemia is also recognized as a serious disorder in many livestock, especially, piglets. We previously studied that the iron-fortified yeast (Saccharomyces cerevisiae) producing Sus scrofa ferritin heavy-chain (FER) was bioavailable to mice with iron deficiency. In this study, we determined whether FER could improve iron deficiency in piglets. The bioavailability of FER was examined by measuring body weight gain, hemoglobin concentration and hematocrit value in suckling and weaning piglets. We found that FER significantly increased hemoglobin value and the hematocrit ratio in suckling piglets (P<0.05). Furthermore, FER treatment significantly enhanced body weight gain in both groups of the suckling and weaning piglets (P<0.05). These results suggest that the iron-fortified recombinant yeast strain is helpful in iron absorption in piglets.

Iron-fortified recombinant Saccharomyces cerevisiae producing Sus scrofa ferritin heavy-chain recovers iron deficiency in mice

  • Lim, Hwan;Kim, Jong-Taek;Kim, Myoung-Dong;Rhee, Ki-Jong;Jung, Bae Dong
    • Korean Journal of Veterinary Research
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    • v.52 no.4
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    • pp.263-268
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    • 2012
  • In this study, we produced iron-fortified yeast (Saccharomyces cerevisiae) producing Sus scrofa ferritin heavy-chain to provide iron supplementation in anemic piglets. We determined whether iron-ferritin accumulated in recombinant yeasts could improve iron deficiency in mice. C57BL/6 male mice exposed to Fe-deficient diet for 2 weeks were given a single dose of ferrous ammonium sulfate (FAS), ferritin-producing recombinant yeast (APO), or APO reacted with iron ($Fe^{2+}$) (FER). The bioavailability of recombinant yeasts was examined by measuring body weight gain, hemoglobin concentration and hematocrit value 1 week later. In addition, ferritin protein levels were evaluated by western blot analysis and iron stores in tissues were measured by inductively coupled plasma spectrometer. We found that anemic mice treated with FER exhibited increased levels of ferritin heavy-chain in spleen and liver. Consistently, this treatment restored the iron concentration in these tissues. In addition, this treatment significantly increased hemoglobin value and the hematocrit ratio. Furthermore, FER treatment significantly enhanced body weight gain. These results suggest that the iron-fortified recombinant yeast strain is bioavailable.

Comparative Study of Enzyme Activity and Stability of Bovine and Human Plasmins in Electrophoretic Reagents, β-mercaptoethanol, DTT, SDS, Triton X-100, and Urea

  • Choi, Nack-Shick;Hahm, Jeung-Ho;Maeng, Pil-Jae;Kim, Seung-Ho
    • BMB Reports
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    • v.38 no.2
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    • pp.177-181
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    • 2005
  • Effects of common electrophoretic reagents, reducing agents ($\beta$-mercaptoethanol [BME] and DTT), denaturants (SDS and urea), and non-ionic detergent (Triton X-100), on the activity and stability of bovine plasmin (b-pln) and human plasmin (h-pln) were compared. In the presence of 0.1% SDS (w/v), all reagents completely inhibited two plns, whereas SDS (1%) and urea (1 M) denatured plns recovered their activities after removal of SDS by treatment of 2.5% Triton X-100 (v/v). However, reducing agents (0.1 M of BME and DTT) treated plns did not restore their activities. Based on a fibrin zymogram gel, five (from b-pln) and four (from h-pln) active fragments were resolved. Two plns exhibited unusual stability in concentrated SDS and Triton X-100 (final 10%) and urea (final 6 M) solutions. Two bands, heavy chain-2 (HC-2) and cleaved heavy chain-2 (CHC-2), of b-pln were completely inhibited in 0.5% SDS or 3 M urea, whereas no significant difference was found in h-pln. Interestingly, 50 kDa (cleaved heavy chain-1, CHC-1) of b-pln and two fragments, 26 kDa (light chain, LC) and 29 kDa (microplasmin, MP), of h-pln were increased by SDS in a concentration dependent manner. We also found that the inhibition of SDS against both plns was reversible.

Association of functional sequence variants of the myosin heavy chain 3 gene with muscle collagen content in pigs

  • Yong-Jun Kang;Sang-Hyun Han;Sang-Geum Kim;Su-Yeon Kim;Hyeon-Ah Kim;Yoo-Kyung Kim;Ji-Hyun Yoo;Moon-Cheol Shin;Byoung-Chul Yang;Hee-Bok Park;Jun Heon Lee;In-Cheol Cho
    • Journal of Animal Science and Technology
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    • v.65 no.3
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    • pp.511-518
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    • 2023
  • This study examined the association between functional sequence variants (FSVs) of myosin heavy chain 3 (MYH3) genotypes and collagen content in a Landrace and Jeju native pig (JNP) crossbred population. Four muscles (Musculus longissimus dorsi, Musculus semimembranosus, Musculus triceps brachii, and Musculus biceps femoris) were used for the analysis of meat collagen content, and the same animals were genotyped for the FSVs of the MYH3 gene by using PCR-RFLP (polymerase chain reaction-restriction fragment length polymorphism). Three FSVs of MYH3 genotypes were identified and had genotype frequencies of 0.358, 0.551, and 0.091 for QQ, Qq, and qq, respectively. QQ animals for the FSVs of the MYH3 genotypes showed higher collagen content in their M. longissimus dorsi (p < 0.001), M. semimembranosus (p < 0.001), M. triceps brachii (p < 0.001), and M. biceps femoris (p < 0.001) than qq homozygous animals. After the validation of this result in other independent populations, the FSVs of MYH3 genotypes can be a valuable genetic marker for improving collagen content in porcine muscles and can also be applied to increase the amount of collagen for biomedical purposes.