• 제목/요약/키워드: non-muscle protein

검색결과 138건 처리시간 0.035초

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

  • 송인선;이석근;손진기
    • 한국발생생물학회지:발생과생식
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    • 제4권1호
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    • pp.67-77
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    • 2000
  • 심해에서 서식하며 특이한 조직형태를 갖고 있는 꼼치조직에서 cDNA를 제작하여 클로닝을 통해서, 꼼치에서 특이하게 발현하는 유전인자를 검색하였다. 그 결과 62례의 클론이 알려진 유전자에 동질성이 있었는데 이들은 thioesterase가 9례, myosin이 8례, creatine kinase가 7례, skeletal alpha-actin이 6례, parvalbumin b와 ribosomal protein이 각각 5례, type I collagen과 muscle troponin이 각각 3례, dopamine receptor, histatin, 그리고 heat shock protein이 각각 2례, cystatin, lectin, statherin, secretory carrier membrane protein, keratin type I, desmin, chloroplast, muscle tropomyosin, reticulum calcium ATPase, ribonucleoprotein이 각각 1례로 나타났다. 나머지 클론은 동질성이 낮거나 비반복성으로 나타났으며, 이 중 in situ hybridization으로 조직에서 특이하게 발현되는 5종류의 클론을 선택하여 분석하였으며, C 말단 단백질 구조와 특색(motif)을 분석하였다. 5종류의 클론에서 C9O-77은 약 5000bp 크기로 상피조직, 점액조직, 섬유조직 그리고 교원질 조직에서 강한 양성반응을 보이는 세포의 기질단백질로 예상되었다. C9O-116은 약 1500bp 크기로 섬유조직, 상피조직 그리고 점액조직에서 약한 양성반응을 보였고, 근육 다발 주변 부위 세포에서 매우 강한 양성반응을 보이는 막투과성 단백질로 예상되었다. C9O-130은 약 1200bp 크기로 상피조직, 근육조직 그리고 점액조직에서 양성반응을 나타냈으며, 특히 상피조직에서 강한 양성반응을 나타내는 세포내 단백질로 예상되었다. C9O-161은 약 2000bp 크기로 상피조직 과 근육조직 그리고 점액성 섬유조직에서 약한 양성반응을 보였고, 상피세포에서 강한 양성반응을 보였으며, 근육다발을 둘러싸는 섬유성 세포에서도 강한 양성반응을 보이는 세포외 기질단백질로 추측되었다. C9O-171은 약 1000bp크기로 상피조직, 근육조직 그리고 섬유기질 조직에 널리 강한 양성반응을 나타냈으며 교원띠조직에서도 양성반응을 보이는 전사인자로 추측되었다.

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

  • 박주동;김진수;조영제;최종덕;최영준
    • 한국식품영양과학회지
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    • 제32권7호
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    • pp.1026-1031
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    • 2003
  • 냉동 백조기로 제조한 알칼리 수리미의 가열 겔 강도 증강을 위한 최적 전분 및 비근육 단백질의 선정과 이들 성분의 최적 첨가량을 설정하기 위해 2수준 fractional factorial과 mixture design을 실시하였으며, 반응 값은 punch test에 의한 물성과 색차계로 색을 측정하였다. 전분은 종류에 관계없이 파괴강도와 변형 값을 감소시켰다. 파괴강도 값은 전분의 농도 증가와 더불어 감소하였고, 변형 값은 유의적인 차이를 보이지 않았다. 비근육 단백질 중 소혈청 단백질이 겔의 파괴강도와 변형 값을 가장 크게 증가시켰으며, 첨가 농도가 증가함에 따라 파괴 강도와 변형 값은 증가하였다. 백색도는 전분과 근육 단백질의 함량이 증가함에 따라 다소 상승하는 것으로 나타났다. 파괴강도 100g 이상, 변형 값 4.6mm이상, 백색도 25.5 이상을 보이는 수리미, 감자전분, 소혈청의 최적 혼합 비율은 각각 89.4∼90.0%, 4.5∼5.2%, 5.3∼5.8%의 범위였다. 전분과 비근육 단백질을 첨가하여 제조한 가열 겔이 단백질의 균일한 분포와 치밀한 망상 구조 형태를 보이고 있었으며 이 같은 구조가 높은 물성 값에 기여하는 것으로 판단하였다.

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

  • Park, Tae Sun
    • Journal of Nutrition and Health
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    • 제28권10호
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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
    • 한국축산식품학회지
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    • 제35권5호
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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.

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

  • 강석용;현선영;권예담;박용기;정효원
    • 대한본초학회지
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    • 제34권6호
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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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    • 제44권4호
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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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    • 제27권9호
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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
    • 한국발생생물학회지:발생과생식
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    • 제23권1호
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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
    • 한국생물물리학회:학술대회논문집
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    • 한국생물물리학회 1996년도 정기총회 및 학술발표회
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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
    • 한국축산식품학회지
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    • 제34권6호
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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.