• 제목/요약/키워드: 7S protein

검색결과 3,259건 처리시간 0.035초

EFFECTS OF DIETARY CELLULOSE AND PROTEIN LEVELS ON NUTRIENT UTILIZATION IN CHICKENS

  • Siri, S.;Tobioka, H.;Tasaki, I.
    • Asian-Australasian Journal of Animal Sciences
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    • 제7권2호
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    • pp.207-212
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    • 1994
  • Effects of dietary cellulose and protein levels on nutrient utilization in chickens were investigated. Four experimental diets containing 5% (low cellulose) or 20% (high cellulose) cellulose in combination with 10% (low protein) or 20% (high protein) protein of 70 g/day were alternatively forced-fed to eight colostomized White Leghorn cockerels once a day to make $4{\times}4$ Latin-square design. The digestibilities of DM and energy decreased with the increase in cellulose level, but not affected by dietary protein level. Ether extract digestibility was higher in the high cellulose diets than in the low cellulose protein level. Ether extract digestibility was higher in the high cellulose diets than in the low cellulose diets. The digestibility of nitrogen free extract had the same trend with the digestibility of DM and energy. The digestibility of acid detergent fiber was not so much different among the diets, but the NDF digestibility was lower in the high cellulose diets than in the low cellulose diets, due to the low hemicellulose digestibility. The true digestibility of protein was influenced by both of the dietary protein and cellulose levels, and their interaction was found. The dietary protein level affected the biological value of protein but the dietary cellulose level did not, and consequently the biological value of protein in the low protein diets was lower than in the high protein diets.

Sasa borealis extract exerts an antidiabetic effect via activation of the AMP-activated protein kinase

  • Nam, Jung Soo;Chung, Hee Jin;Jang, Min Kyung;Jung, In Ah;Park, Seong Ha;Cho, Su In;Jung, Myeong Ho
    • Nutrition Research and Practice
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    • 제7권1호
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    • pp.15-21
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    • 2013
  • Leaf of Sasa borealis, a species of bamboo, has been reported to exhibit anti-hyperglycemic effect. However, its antidiabetic mechanism is not fully understood. In this study, we examined whether an extract of S. borealis activates AMP-activated protein kinase (AMPK) and exerts anti-hyperglycemic effects. Treatment with the S. borealis extract increased insulin signaling and phosphorylation of AMPK and stimulated the expression of its downstream targets, including $PPAR{\alpha}$, ACO, and CPT-1 in C2C12 cells and $PPAR{\alpha}$ in HepG2 cells. However, inhibition of AMPK activation attenuated insulin signaling and prevented the stimulation of AMPK target genes. The S. borealis extract increased glucose uptake in C2C12 cells and suppressed expression of the gluconeogenic gene, PEPCK in HepG2 cells. The extract significantly reduced blood glucose and triglyceride levels in STZ-induced diabetic mice. The extract enhanced AMPK phosphorylation and increased Glut-4 expression in the skeletal muscle of the mice. These findings demonstrated that the S. borealis extract exerts its anti-hyperglycemic effect through activation of AMPK and enhancement of insulin signaling.

유전적 이상에 의한 정신박약자들의 혈액단백질구성 (Composition of Proteins in Mental Retardees Caused by Genetic Disorders)

  • 김강영;김종봉
    • 생명과학회지
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    • 제9권6호
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    • pp.639-645
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    • 1999
  • This research was for investigating the physiological effect caused by genetic disorder and others. Serum protein, serum LDH, and serum CPK were analyzed on Fragile X syndrome patients, carriers, unclassified mental retardees, and Down's syndrome patients by cellulose acetate plate electrophoresis. Also enzyme activity of LDH and CPK were measured. Significant differences were observed between normal group and mental retardees in compositions of serum protein, serum LDH, serum CPK, and enzyme activities. Mean percentages of albumin were 53.70$\pm$7.73% for Fragile X syndrome patients, 57.09$\pm$7.73% for carriers, 47.33$\pm$6.06% for unclassified mental retardees, 50.19$\pm$ 15.72% for Down's syndrome patients. Mean percentages of ${\gamma}$-globulin were 19.64$\pm$6.71% for Fragile X syndrome patients, 19.24$\pm$3.38% for carries, 25.66$\pm$4.74 for unclassified mental retardees, 23.41$\pm$6.08% for Down's syndrome patients. Mean percentages of LDH3 were 27.76$\pm$2.72% for Fragile X syndrome patients, 22.70$\pm$2.76% for carriers, 25.42$\pm$1.26% for unclassified mental retardees, 27.72$\pm$2.58% for Down's syndrome patients. Mean percentages of LDH4 were 2.70$\pm$2.04 for Fragile X syndrome patients, 3.79$\pm$2.74% for carriers, so both of them were significantly lower than normal(P<0.05). Mean percentages of CK-MB were 3.96$\pm$5.56% for Fragile X syndrome patients, 8.80$\pm$7.92%. Mean percentages of CK-MM were 95.81$\pm$5.50% for Fragile X syndrome patients, 91.20$\pm$7.92% for carriers. These results showed that significant abnormal compositions of blood proteins might be caused by genetic disorder. However, further analysis of many patients will be needed for clear conclusion.

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Spectrofluorometric Properties of N-Terminal Domain of Lumazine Protein from Photobacterium leiognathi

  • Kang, Kyoung-Suk;Kim, So-Young;Lee, Jung-Hwan;Nam, Ki-Seok;Lee, Eui Ho;Lee, Chan Yong
    • Bulletin of the Korean Chemical Society
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    • 제34권6호
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    • pp.1673-1678
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    • 2013
  • Lumazine protein is a member of the riboflavin synthase superfamily and the intense fluorescence is caused by non-covalently bound to 6,7-dimethyl 8-ribityllumazine. To figure out the binding modes and the structure of the N-terminal domain of lumazine protein, the wild type of protein extending to amino acid 118 (N-LumP 118 Wt) and mutants of N-LumP 118 V41W, S48W, T50W, D64W, and A66W from Photobacterium leiognathi were purified. The biochemical properties of the wild type and mutants of N-LumP 118 proteins were analyzed by absorbance and fluorescence spectroscope. The peak of absorbance and fluorescence of lumazine ligand were shifted to longer wavelength on binding to N-LumPs. The observed absorbance value at 410 nm of lumazine bound to N-LumP 118 proteins indicate that one mole of N-LumP 118 proteins bind to one mole of ligand of lumazine. Fluorescence analysis show that the maximum peak of fluorescence of N-LumP S48W was shifted to the longest wavelength by binding with 6,7-dimethyl 8-ribityllumazine and was shown to the greatest quench effect by acrylamide among all tryptophan mutants.

Purification and Characterization of Protein Carboxyl O-Methyltransferase from Porcine Spleen

  • Yoon, Sung-Pil;Son, Min-Sik;Han, Jeung-Whan;Lee, Hyang-Woo;Hong, Sung-Youl
    • BMB Reports
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    • 제30권6호
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    • pp.410-414
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    • 1997
  • We purified a protein carboxyl O-methyltransferase (protein methylase II) from porcine spleen to homogeneity. The molecular weight of the porcine spleen protein methylase II (ps-PM II) was estimated to be 27,500 daltons on SDS-PAGE. Amino acid sequence of N-terminal 28 residues for ps-PM II was identified. Amino-terminal three amino acid residues of ps-PM II were deleted when compared to those of other protein carboxyl methytransferase. S-Adenosyl-L-homocysteine competitively inhibits ps-PM II with a K, value of $1.63{\times}10^{-7}M$. Myelin basic protein exhibited the highest methyl-accepting capacity among the proteins tested.

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BMP-2-Enhanced Chondrogenesis Involves p38 MAPK-mediated Down-Regulation of Wnt-7a Pathway

  • Jin, Eun-Jung;Lee, Sun-Young;Choi, Young-Ae;Jung, Jae-Chang;Bang, Ok-Sun;Kang, Shin-Sung
    • Molecules and Cells
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    • 제22권3호
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    • pp.353-359
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    • 2006
  • The bone morphogenetic protein (BMP) family has been implicated in control of cartilage development. Here, we demonstrate that BMP-2 promotes chondrogenesis by activating p38 mitogen-activated protein kinase (MAPK), which in turn downregulates $Wnt-7a/{\beta}$-catenin signaling responsible for proteasomal degradation of Sox9. Exposure of mesenchymal cells to BMP-2 resulted in upregulation of Sox9 protein and a concomitant decrease in the level of ${\beta}$-catenin protein and Wnt-7a signaling. In agreement with this, the interaction of Sox9 with ${\beta}$-catenin was inhibited in the presence of BMP-2. Inhibition of the p38 MAPK pathway using a dominant negative mutant led to sustained Wnt-7a signaling and decreased Sox9 expression, with consequent inhibition of precartilage condensation and chondrogenic differentiation. Moreover, overexpression of ${\beta}$-catenin caused degradation of Sox9 via the ubiquitin/26S proteasome pathway. Our results collectively indicate that the increase in Sox9 protein resulting from downregulation of ${\beta}$-catenin/Wnt-7a signaling is mediated by p38 MAPK during BMP-2 induced chondrogenesis in chick wing bud mesenchymal cells.

LPS로 활성화한 RAW 264.7 세포에서 HK표고버섯균사체의 NF-κB 활성 억제를 통한 항염증 효과 (Anti-inflammatory Efficacy of HK Shiitake Mushroom Mycelium in LPS-treated RAW 264.7 Cells Through Down-regulation of NF-κB Activation)

  • 송채영;오태우;김훈환;이유빈;김정옥;김곤섭;하영래
    • 생명과학회지
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    • 제32권7호
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    • pp.491-500
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    • 2022
  • HK표고버섯균사체(HK shiitake mushroom mycelium, HKSMM)는 간 건강 개별 인정 건강기능식품이다. LPS로 활성화된 RAW 264.7 세포에서 HKSMM50 (HKSMM의 50% ethanol 수용액 추출물)의 항염증효과를 연구하였다. AHCC는 positive control로 사용하였다. LPS로 활성화된 RAW 264.7 세포에 HKSMM50 및 AHCC를 처리(0, 20, 100, 500 ㎍/ml)하고 24시간 배양하여 배양물의 염증 관련 인자는 ELISA kits로, 세포에 함유된 iNOS와 COX-2 protein 발현은 Western blotting으로 측정하였다. HKSMM50는 LPS 처리에 비해 농도 의존적으로 NF-κB 함량을 낮추었고, iNOS와 COX-2 protein 발현을 억제하여 NO와 PGE2 함량을 낮추었다. 더불어 HKSMM50는 LPS 처리에 비해 IL-1β, TNF-α, IL-4 및 IL-6의 함량을 낮추었으나 SOD와 CAT의 활성은 증가시켰다. AHCC도 HKSSM50 처리와 비슷한 효과를 나타내었다. 이 결과는 HKSMM50이 LPS로 활성화된 RAW 264.7 세포에서 NF-κB 신호전달을 억제하여 항염증효과를 나타내었으며, HKSMM은 면역기능증진에 도움을 줄 수 있는 건강기능식품원료로 사용할 수 있을 것이다.

국내 농작물의 근부토양에서 분리한 Pseudomonas 내에서의 Bacillus thuringiensis 독소단백질 유전자의 발현 (Expression of the Bacillus thuringiensis Crystal Protein Gene in Pseudomonas Isolated from Rhizosphere Soil of Korean Crops)

  • Tag, Koo-Bon;Shin, Byung-Sik;Park, Seung-Hwan;Park, Ho-Yong;Kim, Jeong-Il
    • 한국미생물·생명공학회지
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    • 제17권4호
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    • pp.295-300
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    • 1989
  • B. thuringiensis가 생산하는 살충성 독소 단백질의 생태학적 응용방법을 개발하기 위한 목적으로 우선 독소 단백질 유전자를 옮겨 발현시키기에 적합한 숙주 미생물의 분리작업을 수행하였다. 국내 주요농산물인 고추, 감자, 무우 등 7가지 농작물의 뿌리부근에 군락을 형성하는 35종의 형광성Pseudomonas들을 분리하였고 독소 단백질 유전자를 함유하는 재조합 plasmid에 대한 숙주로서의 이응가능성을 검토해 보기 위하여 분리균주 35주에 대한 형질전환을 실시한 결과 4주에 독소 단백질 유전자의 도입이 가능하였고 생물검정과 면역학적인 방법 등에 의한 결과 BT 독소 유전자의 발현을 확인하였다.

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잔디와 시금치의 Thylakoid Membrane으로부터 엽록소-단백질 복합체의 분리와 그 특성 (The Isolation and Characterization of Chlorophyll-Protein Complexes in Thylakoid Membranes from Zoysia japonica and Spinach oleracea)

  • 김병규;장남기
    • 아시안잔디학회지
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    • 제4권1호
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    • pp.12-23
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    • 1990
  • The chlorophyll-protein complexes were separated from thylakoid membranes of Spinach oleracea and Zoysia japonica by two gel Systems of LiDodSO4-PAGE and LiDodSo4/Urea- PAGE under nondenaturing conditions. Seven chlorophyll~protein complexes of CPI*, CPI, CPII*. CP47, CP43, CP29 and CPII were fractionated from both S,oleracea and Zjaponica by LiDodSO4-PAGE. CPI, CP47 and CP43 contained more chlorophyll a than chlorophyll b. The patterns of their absorption spectra at room temperature were similliar to that of chlorophyll a, judging by their UV-spedtroscopy. On the other hand, CPII* and CPII contained approximately equim-olar quantities of chlorophyll a and b. Additional five chlorophyll-protein complexes not separated in the LiDodSO4-PAGE system were electrophoretically isolated from both S, oleracea and Zjaponica by LiDodSO4/Urca-PAGE. The chlorophyll-protein complex just above LRCII $\alpha$in the gel appears CCII-RC separeted recently. 23 kDa and 20 kDa cho-protein complexes is probably LHCIa and LHCIb as judged from their molecular weight. Two novel chlorophyll~protein complexes designated "CPI7" and "CPI6" were fractionate by this gel system. Their molecular weights respectively. Although the stoichiometry of their components and their roles in thylakoid membranes are not apparant, It is thought that they are another kinds of LHCI.other kinds of LHCI.

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단백질 추출용 역미셀 실관막장치에 관한 연구 (Reversed Micellar Protein Extraction in a Hollow Fiber Membrane Extractor)

  • 윤현희;박상준유인상
    • KSBB Journal
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    • 제9권3호
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    • pp.332-338
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    • 1994
  • 역미생용액으로 단백칠을 추출하는 공정에셔 수용 액의 이온세기와 pH가 중요한 공정변수가 된다. 본 실험에셔 사용한 역미생용액은 AOT를 Isooctane에 5 50mM의 농도로 용해시켜 사용하였고 단백칠로서 alkaline protease를 model compound로 사용하여 추출설험을 수행한 결과 본 설험의 범위에서 pH가 낮을수록, 이온세기가 낮을수록 효율적인 추출이 이루어졌으며, pH가 3.0 그리고 이온세기가 O.lM KCI 일때 분배계수가 4.0으로 가장 크게 나타났다. 단백질의 용매추출 장치로서 설관막 모률을 제작 하여 alkaline protease를 역미생을 이용하여 용매 추출을 수행하였는 바, 단백질 분리공정에 효과적인 장치로 사용될 수 었음을 보여주였다. 본 실험의 조 건에서 총괄물질전달계수 Ko가 $6.7{\times}10^{-5}cm/s$이었으며 유기용매상의 개별물칠전달저항이 수용액상의 물질전달저항보다 중요하게 나타났다. 실관막 추출 장치의 조업시 설관막 양쪽 상의 압력차를 $0.1kg/cm^2$. 이하로 조절하여 emulsion의 형성을 방지할 수 있었다.

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