• Title/Summary/Keyword: non-muscle protein

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Molecular Cloning of Novel Genes Specifically Expressed in Snailfish, Liparis tanakae (꼼치, Liparis tanakae에서 특이하게 발현되는 새로운 유전인자의 검색)

  • 송인선;이석근;손진기
    • Development and Reproduction
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    • v.4 no.1
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    • pp.67-77
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    • 2000
  • Snailfish usually lives at the bottom of the sea and showed typical retrogressive change with specialized tissue structures of skin and skeletons. In order to obtain the specific genes of snailfish, highly expressed in the body, we made subtracted cDNA library and analyzed 200 clones. Totally 200 clones were obtained and sequenced, and among them 62 clones were turned out to be homologous to the known gene, i.e., thioesterase (9), myosin (8), creatine kinase (7), skeletal alpha-actin (6), parvalbumin b (5), ribosomal protein (5), type I collagen (3), muscle troponin (3), dopamine receptor (2), histatin (2), and heat shock protein (2), cystatin (1), lectin (1), statherin (1), secretory carrier membrane protein (1), keratin type I (1), desmin (1), chloroplast (1), muscle tropomyosin (1), reticulum calcium ATPase (1), ribonucleoprotein (1). The remaining 138 clones were low homologous or non-redundant genes through Genbank search. Especially 5 clones were novel and specifically expressed in the body tissues of Snailfish by in situ hybridization. Therefore, we analysed these 5 clones to identify the C-terminal protein structures and motifs, and partly defined the roles of these proteins in comparison with the expression patterns by in situ hybridization. C9O-77, about 5000 bp, was supposed to be a matrix protein expressed strongly positive in epithelium, myxoid tissue, fibrous tissue and collagenous tissue. C9O-116, about 1500 bp, was supposed to be a transmembrane protein which was weakly expressed in the fibrous tissue, epithelium tissue, and myxoid tissue, but strong in muscle tissue. C9O-130, about 1200 bp, was supposed to be an intracytoplasmic molecule usually in the epithelial cells. C9O-161, about 2000 bp, was weakly expressed in epithelium, muscle tissue and myxoid tissue, but specially strong in epithelium. C9O-171, about 1000 bp, was supposed to be a transcription factor containing zinc finger like domain, which was intensely expressed in the epithelium, muscle tissue, fibrous tissue, and in collagenous tissue.

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Optimum Formulation of Starch and Non-muscle Protein for Alkali Surimi Gel from Frozen White Croaker (냉동 백조기의 알칼리 수리미 겔 제조를 위한 전분 및 비근육 단백질의 최적화)

  • 박주동;김진수;조영제;최종덕;최영준
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.32 no.7
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    • pp.1026-1031
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    • 2003
  • The two-level full factorial and mixture design were used to screen ingredient type and to investigate effects of ingredients on properties of alkali surimi gel from frozen white croakers using measurements of a breaking force, deformation and color. The addition of starch decreased a breaking force and deformation of gel regardless of starch type. The breaking force was decreased, but a deformation was not significantly changed (p<0.05) with increasing starch level. The potato starch was more resonable than com and wheat starch for a breaking force and deformation. The bovine plasma protein (BPP) greatly improved a breaking force and deformation. The breaking force and deformation of gel were increased with concentration of BPP. The whiteness of gel was slightly improved with adding starch and non-muscle for all treatments. At 78% moisture, the optimum ratios of ingredients were 89.4∼90.0% for surimi, 5.9∼6.3% for potato starch and 5.0∼5.4% for BPP to obtain above 100g for a breaking force, 4.6 mm for a deformation, and 25.5 for a whiteness.

Changes in Blood and Tissue Free Amino Acid Concentrations in Cats Adapted to Low-and High-protein Diets (단백질 섭취 수준에 따른 고양이의 혈액 및 조직의 유리 아미노산 농도의 변화)

  • Park, Tae Sun
    • Journal of Nutrition and Health
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    • v.28 no.10
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    • pp.976-985
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    • 1995
  • Changes in free amino acid concentrations is blood and various tissues were evaluated in cats adapted to the low-protein diet(20% protein, LPD) or the high-protein diet(60% protein, HPD) for 5 weeks. Cumulative body weigth gain for the 5 week period was 463$\pm$43g, and -128$\pm$40g for cats fed HPD and LPD, respectively. Feeding HPD significantly increased the size of liver and kidney. Cats adapted to HPD for 5 weeks have significantly elevated plasma concrntrations of essential amino acids (branched-chain amino acides, threonine, trytophan, phenylalanine and methoionine), whereas plasma levels of non-essential amino acids(alanine, asparagine, glycine, glutamine and serine) were significantly reduced in animals adapted to HPD(p<0.01, or p<0.001) compared to the values for the cats fed LPD. Changes in free amino acid concentratioks in whole blood induced by the variations in dietary level of protein closely reflect the pattern seen in plasma. Amino acids such as branched-chain amino acids, proline and threonine were most difficult to maintain homeostasis and consistantly elevated in lever, kidney, skeletal muscle and brain, as well as in blood of cats adapted to HPD(p<0.01 or p<0.001). All of the free amino acids in jejunum, excluding taurine and ornithine, were significantly elevated in animals adapted to HPD, most probably due to the rapid absorption of large amount of amino acids across the epithelium of small intestine.

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Effect of Pre-rigor Salting Levels on Physicochemical and Textural Properties of Chicken Breast Muscles

  • Kim, Hyun-Wook;Hwang, Ko-Eun;Song, Dong-Heon;Kim, Yong-Jae;Ham, Youn-Kyung;Yeo, Eui-Joo;Jeong, Tae-Jun;Choi, Yun-Sang;Kim, Cheon-Jei
    • Food Science of Animal Resources
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    • v.35 no.5
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    • pp.577-584
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    • 2015
  • This study was conducted to evaluate the effect of pre-rigor salting level (0-4% NaCl concentration) on physicochemical and textural properties of pre-rigor chicken breast muscles. The pre-rigor chicken breast muscles were de-boned 10 min post-mortem and salted within 25 min post-mortem. An increase in pre-rigor salting level led to the formation of high ultimate pH of chicken breast muscles at post-mortem 24 h. The addition of minimum of 2% NaCl significantly improved water holding capacity, cooking loss, protein solubility, and hardness when compared to the non-salting chicken breast muscle (p<0.05). On the other hand, the increase in pre-rigor salting level caused the inhibition of myofibrillar protein degradation and the acceleration of lipid oxidation. However, the difference in NaCl concentration between 3% and 4% had no great differences in the results of physicochemical and textural properties due to pre-rigor salting effects (p>0.05). Therefore, our study certified the pre-rigor salting effect of chicken breast muscle salted with 2% NaCl when compared to post-rigor muscle salted with equal NaCl concentration, and suggests that the 2% NaCl concentration is minimally required to ensure the definite pre-rigor salting effect on chicken breast muscle.

Effects of Chaenomelis Fructus Extract on the regulation of myoblasts differentiation and the expression of biogenetic factors in C2C12 myotubes (모과추출물의 C2C12 근육세포에서 근분화 및 에너지대사조절인자 발현 증진 효과 연구)

  • Kang, Seok Yong;Hyun, Sun Young;Kwon, Yedam;Park, Yong-Ki;Jung, Hyo Won
    • The Korea Journal of Herbology
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    • v.34 no.6
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    • pp.99-107
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    • 2019
  • Objective : The present study was conducted to investigate the effects of Chaenomelis Fructus (CF) on the regulation of biogenesis in C2C12 mouse skeletal muscle cells. Methods : C2C12 myoblasts were differentiated into myotubes in 2% horse serum-containing medium for 5 days, and then treated with CF extract at different concentrations for 48 hr. The expression of muscle differentiation markers, myogenin and myosin heavy chain (MHC) and mitochondrial biogenesis-regulating factors, peroxisome proliferator-activated receptor gamma coactivator 1alpha (PGC1α), sirtuin1 (Sirt1), nuclear respiratory factor1 (NRF1) and transcription factor A, mitochondrial (TFAM), and the phosphorylation of AMP-activated protein kinase (AMPK) and acetyl-CoA carboxylase (ACC) were determined in C2C12 myotubes by reverse transcriptase (RT)-polymerase chain reaction (RT-PCR) and western blot, respectively. The cellular glucose levels and total ATP contents were measured by cellular glucose uptake and ATP assays, respectively. Results : Treatment with CF extract (0.01, 0.02, and 0.05 mg/㎖) significantly increased the expression of MHC protein in C2C12 myotubes compared with non-treated cells. CF extract significantly increased the expression of PGC1α and TFAM in the myotubes. Also, CF extract significantly increased glucose uptake levels and ATP contents in the myotubes. Conclusion : CF extract can stimulate C2C12 myoblasts differentiation into myotubes and increase energy production through upregulation of the expression of mitochondrial biogenetic factors in C2C12 mouse skeletal muscle cell. This suggests that CF can help to improve skeletal muscle function with stimulation of the energy metabolism.

Improved recovery of active GST-fusion proteins from insoluble aggregates: solubilization and purification conditions using PKM2 and HtrA2 as model proteins

  • Park, Dae-Wook;Kim, Sang-Soo;Nam, Min-Kyung;Kim, Goo-Young;Kim, Jung-Ho;Rhim, Hyang-Shuk
    • BMB Reports
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    • v.44 no.4
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    • pp.279-284
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    • 2011
  • The glutathione S-transferase (GST) system is useful for increasing protein solubility and purifying soluble GST fusion proteins. However, purifying half of the GST fusion proteins is still difficult, because they are virtually insoluble under non-denaturing conditions. To optimize a simple and rapid purification condition for GST-pyruvate kinase muscle 2 (GST-PKM2) protein, we used 1% sarkosyl for lysis and a 1 : 200 ratio of sarkosyl to Triton X-100 (S-T) for purification. We purified the GST-PKM2 protein with a high yield, approximately 5 mg/L culture, which was 33 times higher than that prepared using a conventional method. Notably, the GST-high-temperature requirement A2 (GST-HtrA2) protein, used as a model protein for functional activity, fully maintained its proteolytic activity, even when purified under our S-T condition. This method may be useful to apply to other biologically important proteins that become highly insoluble in the prokaryotic expression system.

The Effects of Vitamin B6 Deficiency on Stored Fuel Utilization During 3 days Fasting or 6 days underfeeding in Rats

  • Cho, Youn-Ok
    • Journal of Nutrition and Health
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    • v.27 no.9
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    • pp.923-929
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    • 1994
  • The effects of vitamin B6 deficiency on energy utilization during fasting or underfeeding were studied in rats. Fifteen rats were fed a vitamin B6 deficient(-B6) diet and another 15 rats wee fed a control (+B6) diet. These rats were fed for 5 weeks with respective diet, and then subdivided into 3 groups : non-fasted group, fasted group, underfed group. Rats of the fasted group were fasted for 3 days and those of underfed group for 6 days. At the respective time (non-fast, 3 day-fast, 6 day-underfeed at 5 weeks), animals were sacrificed. Feed efficiency ratio of - B6 rats was significantly lower than that of +B6 rats. In - B6 rats, the liver and kidney weights were significantly heavier than those of +B6 rats but spleen and heart weights were not. In non-fasted group, liver protein and triglyceride level of - B6 rats were significantly higher than that of +B6 rats. After - B6 rats were fasted for 3 days, plasma free fatty acid level was significantly lower but liver glycogen level was higher than that of +B6 rats and muscle protein level of +B6 was decreased while that of - B6 was not changed. Vitamin B6 deficiency had little effect on the energy utilization with 6 days underfeeding. These results suggest that vitamin B6 deficiency may impair the utilization of stored fuel during fasting.

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The Regulatory Region of Muscle-Specific Alpha Actin 1 Drives Fluorescent Protein Expression in Olive Flounder Paralichthys olivaceus

  • Kong, Hee Jeong;Kim, Julan;Kim, Ju-Won;Kim, Hyun-Chul;Noh, Jae Koo;Kim, Young-Ok;Kim, Woo-Jin;Yeo, Sang-Yeob;Park, Jung Youn
    • Development and Reproduction
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    • v.23 no.1
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    • pp.55-61
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    • 2019
  • To develop a promoter capable of driving transgene expression in non-model fish, we identified and characterized the muscle-specific alpha-actin gene in olive flounder, Paralichthys olivaceus (PoACTC1). The regulatory region of PoACTC1 includes putative regulatory elements such as a TATA box, two MyoD binding sites, three CArG boxes, and a CCAAT box. Microinjection experiments demonstrated that the regulatory region of PoACTC1, covering from -2,126 bp to +751 bp, just prior to the start codon, drove the expression of red fluorescent protein in developing zebrafish embryos and hatching olive flounder. These results suggest that the regulatory region of PoACTC1 may be useful in developing a promoter for biotechnological applications such as transgene expression in olive flounder.

DIRECT MODULATI6ON OF MAXI-K CHANNEL IN SMOOTH MUSCLE CELL

  • Lee, Moo-Yeol;Chung, Sung-Kwon;Bang, Hyo-Weon;Uhm, Dae-Yong
    • Proceedings of the Korean Biophysical Society Conference
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    • 1996.07a
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    • pp.36-36
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    • 1996
  • The activities of Maxi-K channels were recorded using inside-out patches. The application of 30 nM of non-specific G protein activator, GTP $\gamma$S, to the intracellular side of the channels increases the channel activities about 3-fold, indicating that there exist some G proteins within the patch membranes to regulate the channel activities. (omitted)

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Skeletal Muscle Troponin I (TnI) in Animal Fat Tissues to Be Used as Biomarker for the Identification of Fat Adulteration

  • Park, Bong-Sup;Oh, Young-Kyoung;Kim, Min-Jin;Shim, Won-Bo
    • Food Science of Animal Resources
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    • v.34 no.6
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    • pp.822-828
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    • 2014
  • In this study, the existence of skeletal muscle troponin I (smTnI), well-known as a muscle protein in fat tissues, and the utilization of smTnI as a biomarker for the identification of fat adulteration were investigated. A commercial antibody (ab97427) specific to all of animals smTnI was used in this study. Fat and meat samples (cooked and non-cooked) of pork and beef, and chicken considered as representative meats were well minced and extracted by heating and non-heating methods, and the extracts from fat and meat tissues were probed by the antibody used in both enzyme-linked immunosorbent assay (ELISA) and immunoblot. The antibody exhibited a strong reaction to all meat and fat extracts in ELISA test. On the other hand, the results of immunoblot analsis revealed a 23 kDa high intensity band corresponding to the molecular weight of smTnI (23786 Da). These results demonstrate that the existence of smTnI in all animal fat tissues. Since there are monoclonal antibodies specific to each species smTnI, smTnI in fat tissues could be used as a biomarker to identify or determine animal species adulterated in meat products. Therefore, an analytical method to identify fraudulent fat adulteration can be developed with an antibody specific to each species smTnI.