• Title/Summary/Keyword: NP protein

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Physiological and Proteomics Analysis to Potassium Starvation in Rice

  • Kim, Sang-Gon;Wang, Yiming;Lee, Chang-Hoon;Chi, Yong-Hun;Kim, Keun-Ki;Choi, In-Soo;Kim, Yong-Chul;Kang, Kyu-Young;Kim, Sun-Tae
    • Korean Journal of Environmental Agriculture
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    • v.30 no.4
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    • pp.395-401
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    • 2011
  • BACKGROUND: Potassium (K) is one of the macronutrients which are essential for plant growth and development. Its deficiency in paddy soils is becoming one of the limiting factors for increasing rice yield in Asia. METHODS AND RESULTS: To investigate physiological symptoms under K-starvation (NP) compared with complete media (NPK) condition, we measured shoot/root length, weight, nutrients, and patterns of protein expression. The shoot growth was significantly reduced, but root growth was not affected by K-starvation. However, biomasses were decreased in both shoot and root. Uptake of K was reduced up to 85%, while total concentrations of P, Ca, Mg, Na were increased in root and shoot. To better understand the starved K mechanism of rice, comparative proteome analysis for proteins isolated from rice leaves was conducted using 2-DGE. Five spots of differentially expressed proteins were analyzed by MALDI-TOF MS. Analysis of these K-starvation response proteins suggested that they were involved in metabolism and defense. CONCLUSION(s): Physiological and 2-DGE based proteomics approach used in our study results in observation of morphology or nutrients change and identification of K-starvation responsive proteins in rice root. These results have important roles in maintaining nutrient homeostasis and would also be useful for further characterization of protein function in plant K nutrition.

The Effect of Junci Medulla Herbal-acupuncture at $KI_{10}$ on LPS induced Nephritis in Rats (음곡에 시술한 등심초약침이 LPS로 유도된 흰쥐의 신장염에 미치는 영향)

  • Ihm, Jee Soon;Cho, Tae Hwan;Yim, Yun Kyoung
    • Journal of Acupuncture Research
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    • v.29 no.6
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    • pp.73-83
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    • 2012
  • Objectives : This study aimed to evaluate the effects of Junci Medulla Herbal-acupuncture(JM-HA) at $KI_{10}$(Umgok) on nephritis induced by lipopolysaccharide(LPS) in rats. Methods : Rats with nephritis induced by LPS, were treated with JM-HA at $KI_{10}$ 3 times a week. The rats in the NP group and the saline group were treated with a needle prick and a saline injection respectively. To evaluate the effects of JM-HA at $KI_{10}$ on nephritis in rats, WBC, neutrophils in blood, BUN, creatinine, TNF-${\alpha}$ in serum, creatinine, total protein in urine and renal MPO were measured. Results : JM-HA at $KI_{10}$ significantly inhibited the increase of WBC and neutrophils in blood, BUN, creatinine, TNF-${\alpha}$ in serum, and MPO in kidney of LPS-stimulated rats. Conclusion : JM-HA at $KI_{10}$ has therapeutic effects on nephritis in LPS-stimulated rats. Therefore, it is suggested that JM-HA at $KI_{10}$ may be a useful therapy in clinical field after further researches.

Anti-inflammatory Effect on Desmodii Herba Pharmacopuncture at $KI_{10}$ on Nephritis in Rats (음곡 금전초약침이 LPS로 유도된 흰쥐의 신장염에 미치는 영향)

  • Yoon, Kwang-Shik;Kang, Jae-Hui;Lee, Hyun
    • Journal of Acupuncture Research
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    • v.28 no.3
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    • pp.43-54
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    • 2011
  • Objectives : This study was designed to evaluate the effects of Desmodii herb pharmacopuncture (DH-HA) at $KI_{10}$(Umgok) on nephritis induced by lipopolysaccharide(LPS) in rat. Methods : Rats were injected LPS to induce nephritis. DH-HA group was treated with DH-HA at $KI_{10}$ three times for a week, NP group with 26 gauge needle, saline group with normal saline. To evaluate the effects of DH-HA at $KI_{10}$ on nephritis in rats, RBC, WBC, neutrophil in blood, TNF-a, CINC-1 in serum, creatinine and total protein in urine, renal TNF-a, renal MPO were measured and renal tissue was analyzed. Results : WBC in blood, CINC-1 in serum, renal MPO significantly reduced in DH-HA group. Conclusions : DH-HA at $KI_{10}$ is effective for nephritis in LPS-induced rats. Therefore, DH-HA at $KI_{10}$ may be useful for nephritis in clinical field.

BIOCHEMICAL POLYMORPHISM STUDIES IN BREEDS OF WOOL-SHEEP, HAIR-SHEEP AND THEIR HYBRIDS IN MALAYSIA

  • Lee, S.L.;Mukherjee, T.K.;Agamuthu, P.;Panandam, J.M.
    • Asian-Australasian Journal of Animal Sciences
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    • v.8 no.4
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    • pp.357-364
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    • 1995
  • A biochemical genetic study on blood enzyme/protein systems in some breeds/crosses of sheep in Malaysia was carried out using horizontal starch gel electrophoresis. Blood samples were collected from 435 sheep, representing 8 breeds/crosses. These included 5 wool sheep breeds (Thai Longtail, wiltshire, Suffolk, Dorsimal and cMBLx), 1 hair sheep breed (Barbados Blackbelly) and 2 hybrids between wool sheep and hair sheep (Cameroon ${\times}$ Thai Longtail and Bali Bali ${\times}$ Malin). Twenty loci systems were examined. Of these, ten ($HB{\beta}$, ALB, TF, XP, CAT, DIA1, EsA, GPI, ME and NP) exhibited genetic variation whereas the other ten (AAT, CA, DIA2, ${\alpha}GLO$, ${\alpha}GLU$, LDH, MDH, PEP[leu-gly-gly], 6PGD and SOD) were monomorphic. The allelic frequencies which were obtained in 10 polymorphic markers are assessed and compared with the results obtained by previous workers. The estimations of inbreeding coefficient, intrabreed variation and breed relationships have been critically discussed and are used to reveal some important recommendations.

Determination of $K^+-, Ca^{2}+- and Mg^{2+}-$ATPase activities in Fish Muscle Protein by ATPase Biosensor (ATPase 센서를 이용한 어류근육 단백질의 $K^+-, Ca^{2}+- 및 Mg^{2+}-$ ATPase 활성의 측정)

  • 천병수;김희경
    • KSBB Journal
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    • v.11 no.5
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    • pp.518-523
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    • 1996
  • The sensor to determine ATPase activities was consisted of an immobilized enzyme membrane(purine nucloside phosphoryrase and xanthine oxidase) and an oxygen electrode. The proposed sensor was used for the determination of $K^+-, Ca^{2}+- and Mg^{2+}-$ATPase activities in several fish muscle proteins such as Thunnus albacares(Yellowfin tuna), Tetrapturus audax(Striped marlin), Prognichthys agoo(Japanese flyingfish), and Cypvinus carpio(Carp). $K^+-, Ca^{2}-$ATPase activities measured by the proposed sensor system were in good agreement with the results obtained by a conventional colorimetric assay. One cycle of assay could be completed within 3mlnutes.

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Protective Effects of Thiazolo[3,2-b]-1,2,4-Triazoles on Ethanol­Induced Oxidative Stress in Mouse Brain and Liver

  • Aktay Goknur;Tozkoparan Birsen;Ertan Mevlut
    • Archives of Pharmacal Research
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    • v.28 no.4
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    • pp.438-442
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    • 2005
  • A series of 3-[1-(4-(2-methylpropyl) phenyl) ethyl]-1,2,4-triazole-5-thione (I) and its bicyclic condensed derivatives 6-benzylidenethiazolo[3,2-b]-1, 2,4-triazole-5(6H)-ones (IIa-IIf) were investigated for the prevention of ethanol-induced oxidative stress in liver and brain of mice. Administration of ethanol (0.1 mL/mice, p.o.) resulted in a drop of total thiol groups (T-SH) and non-protein thiol groups (NP-SH), and an increase in thiobarbituric acid reactive substances (TBARS) in both liver and brain tissue of mice (p<0.001). Among the compounds investigated (at a dose of 200 mg/kg, p.o.), I and IId ameliorated the peroxidative injury in these tissues effectively. Compounds IIa, IIc and IIe improved the peroxidative tissue injury only in brain. These findings suggest that certain condensed thiazolo-triazole compounds may contribute to the control of ethanol-induced oxidative stress in an organ selective manner.

A Simple and Rapid Methicillin-Resistant Staphylococcus aureus (MRSA) Screening Test Using a Mannose-Binding Lectin (MBL)-Conjugated Gold Nanoparticle Probe

  • So Yeon Yi;Jinyoung Jeong;Wang Sik Lee;Jungsun Kwon;Kyungah Yoon;Kyoungsook Park
    • Journal of Microbiology and Biotechnology
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    • v.33 no.5
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    • pp.698-705
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    • 2023
  • Rapid diagnosis of methicillin-resistant Staphylococcus aureus (MRSA) is essential for guiding clinical treatment and preventing the spread of MRSA infections. Herein, we present a simple and rapid MRSA screening test based on the aggregation effect of mannose-binding lectin (MBL)-conjugated gold nanoparticles (AuNP), called the MRSA probe. Recombinant MBL protein is a member of the lectin family and part of the innate immune system. It can recognize wall teichoic acid (WTA) on the membrane of MRSA more specifically than that of methicillin-sensitive Staphylococcus aureus (MSSA) under optimized salt conditions. Thus, the MRSA probe can selectively bind to MRSA, and the aggregation of the probes on the surface of the target bacteria can be detected and analyzed by the naked eye within 5 min. To demonstrate the suitability of the method for real-world application, we tested 40 clinical S. aureus isolates (including 20 MRSA specimens) and recorded a sensitivity of 100%. In conclusion, the MRSA probe-based screening test with its excellent sensitivity has the potential for successful application in the microbiology laboratory.

Characterization of a Chitinase Gene and Screening of Cold Active Chitinase from Polar Microorganisms (극지유래 저온활성 Chitinase 생산균주의 스크리닝과 Chitinase 유전자 클로닝)

  • Park, Yu Kyung;Kim, Jung Eun;Lee, Hyoungseok;Kim, Ji Hyun;Park, Ha Ju;Kim, Dockyu;Park, Mira;Yim, Joung Han;Kim, Il-Chan
    • Korean Journal of Microbiology
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    • v.48 no.4
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    • pp.293-297
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    • 2012
  • Of the 169 strains of microorganisms stored in Polar and Alpine Microbial Collection of Korea Polar Research Institute, 27 strains were selected for their chitinase activity on ZoBell plates supplemented with 0.4% colloidal chitin. Among them, PAMC 21693 strain have shown the highest chitinolytic enzyme activity toward pNP-$(GlcNAc)_1$ at low temperature and the highest growth rate at $4^{\circ}C$. We cloned a full-length chitinase gene of 2,857 bp which contains an open reading frame of 2,169 bp encoding 872-amino acid polypeptide. Recombinant chitinase protein was expressed in E. coli and its molecular weight was confirmed 96 kDa. In this paper, we suggest the potential use of cold-active chitinase from polar microorganisms in the field of biotechnology.

Gene Cloning and Characterization of a Cold-Adapted Esterase from Acinetobacter venetianus V28

  • Kim, Young-Ok;Heo, Yu Li;Kim, Hyung-Kwoun;Nam, Bo-Hye;Kong, Hee Jeong;Kim, Dong-Gyun;Kim, Woo-Jin;Kim, Bong-Seok;Jee, Young-Ju;Lee, Sang-Jun
    • Journal of Microbiology and Biotechnology
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    • v.22 no.9
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    • pp.1245-1252
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    • 2012
  • Acinetobacter venetians V28 was isolated from the intestine of righteye flounder, Poecilopsetta plinthus caught in Vietnam seawater, and the esterase gene was cloned using a shotgun method. The amino acid sequence deduced from the nucleotide sequence (1,017 bp) corresponded to a protein of 338 amino acid residues with a molecular weight of 37,186. The esterase had 87% and 72% identities with the lipases of A. junii SH205 and A. calcoaceticus RUH2202, respectively. The esterase contained a putative leader sequence, as well as the conserved catalytic triad (Ser, His, Asp), consensus pentapeptide GXSXG, and oxyanion hole sequence (HG). The protein from the strain V28 was produced in both a soluble and an insoluble form when the Escherichia coli cells harboring the gene were cultured at $18^{\circ}C$. The maximal activity of the purified enzyme was observed at a temperature of $40^{\circ}C$ and pH 9.0 using p-NP-caprylate as substrate; however, relative activity still reached to 70% even at $5^{\circ}C$ with an activation energy of 3.36 kcal/mol, which indicated that it was a cold-adapted enzyme. The enzyme was a nonmetallo-protein and was active against p-nitrophenyl esters of $C_4$, $C_8$, and $C_{14}$. Remarkably, this enzyme retained much of its activity in the presence of commercial detergents and organic solvents. This cold-adapted esterase will be applicable as catalysts for reaction in the presence of organic solvents and detergents.

Development of a Simple and Reproducible Method for Removal of Contaminants from Ginseng Protein Samples Prior to Proteomics Analysis (활성탄을 이용한 불순물제거에 의한 효과적인 인삼 조직 단백질체 분석 방법 개선 연구)

  • Gupta, Ravi;Kim, So Wun;Min, Chul Woo;Sung, Gi-Ho;Agrawal, Ganesh Kumar;Rakwal, Randeep;Jo, Ick Hyun;Bang, Kyong Hwan;Kim, Young-Chang;Kim, Kee-Hong;Kim, Sun Tae
    • Journal of Life Science
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    • v.25 no.7
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    • pp.826-832
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    • 2015
  • This study describes the effects of activated charcoal on the removal of salts, detergents, and pigments from protein extracts of ginseng leaves and roots. Incubation of protein extracts with 5% (w/v) activated charcoal (100-400 mesh) for 30 min at 4℃ almost removed the salts and detergents including NP-40 as can be observed on SDS-PAGE. In addition, analysis of chlorophyll content showed significant depletion of chlorophyll (~33%) after activated charcoal treatment, suggesting potential effect of activated charcoal on removal of pigments too along with the salts and detergents. 2-DE analysis of activated charcoal treated protein samples showed better resolution of proteins, further indicating the efficacy of activated charcoal in clearing of protein samples. In case of root proteins, although not major differences were observed on SDS-PAGE, 2-DE gels showed better resolution of spots after charcoal treatment. In addition, both Hierarchical clustering (HCL) and Principle component analysis (PCA) clearly separated acetone sample from rest of the samples. Phenol and AC-phenol samples almost overlapped each other suggesting no major differences between these samples. Overall, these results showed that activated charcoal can be used in a simple manner to remove the salts, detergents and pigments from the protein extracts of various plant tissues.