• Title/Summary/Keyword: Ion gel

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Immunocytochemical Localization of Vicilin in Endosperm Cells of Panax ginseng C.A. Meyer (인삼(Panax ginseng C.A. Meyer) 배유세포내 Vicilin의 면역세포화학적 분포)

  • 이창섭
    • Journal of Plant Biology
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    • v.35 no.2
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    • pp.99-106
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    • 1992
  • The endosperm protein, vicilin, of ginseng (Panax ginseng C.A. Meyer) was purified by ammonium sulfate precipitaion, gel permeation and ion exchange column chromatography. Vicilin is a glycoprotein composed of 2 subunits with molecular masses of 55,000 (large subunit) and 44,000 (small subunit). The anti-vicilin antibody was raised in rabbit, and purified by DEAE Affi-Gel Blue affinity chromatography. The endosperm cells of the seed were reacted with this anti-vicilin antibody and colloidal gold conjugated secondary antibody. Gold particles were labelled on the elaborating granules of Golgi complex, electron-dense granules and protein bodies in the endosperm cells. These results indicated that the vicilin, which was synthesized in rough endoplasmic reticulum and transported to Golgi, was elaborated in saccules of the Golgi and then transported into protein bodies by electron-dense granules.anules.

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Purification and Characterization of Intracellular Cellulase from Aspergillus oryzae ITCC-4857.01

  • Begum, Ferdousi;Absar, Nurul
    • Mycobiology
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    • v.37 no.2
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    • pp.121-127
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    • 2009
  • Purification and characterization of intracellular cellulase produced by A. oryzae ITCC-4857.01 are reported. The enzyme was purified by ion-exchange chromatography using DEAE-cellulose followed by Gel filtration. The purification achieved was 41 fold from the crude extract with yield of 27%. The purified enzyme showed single band on poly acrylamide gel. The molecular weight as determined by SDS-PAGE and gel filtration was 38 KDa and 38.6 KDa respectively and contained only one subunit. The enzyme is glycoprotien as nature and contained 0.67% neutral sugar. The apparent Km value of the enzyme against cellulose was 0.83%. The enzyme showed the highest relative ativities on CMC followed by avicel, salicin and filter paper. The optimum pH of activity was 5.5 and very slight activity was observed at or above pH 7.5 as well as bellow pH 3.5. The optimum tempreture of the activity was $45^{\circ}C$ and the highest activity was exhibited in 35 to $45^{\circ}C$. The enzyme lost their activities almost completely (95${\sim}$100%) at $80^{\circ}C$ or above and as well as bellow $25^{\circ}C$.

Oxidation of Primary Alcohol Groups of Polysaccharides with 2,2,6,6-Tetramethyl-1-Piperidine Oxoammonium Ion (2,2,6,6-Tetramethyl-1-Piperidine Oxoammonium Ion에 의한 다당류내 1차 알코올의 특이적 산화)

  • Chang, Pahn-Shick;Cho, Gye-Bong
    • Korean Journal of Food Science and Technology
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    • v.29 no.3
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    • pp.446-451
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    • 1997
  • The primary alcohol groups of four kinds of polysaccharides (com starch, rice starch, sweet potato starch, and cellulose), with different structures and water solubilities, were oxidized to carboxyl groups using 2,2,6,6-tetramethyl-1-piperidine oxoammonium ion (TEMPO) at $25^{\circ}C$. The optimum pH, TEMPO content, and NaBr content for the TEMPO/hypobromite-catalyzed oxidation of the polysaccharides were $10.5{\sim}11.0$, 10 mmol/mol primary alcohol, and 0.49 mmol/mol primary alcohol, respectively. The oxidation degree for the primary alcohol group was more than 90% for all four kinds of the polysaccharides. The oxidation process greatly increased the water solubility of the polysaccharides. Water-insoluble polysaccharide such as cellulose became water-soluble to the extent of 8.42% (w/v). And also, the polysaccharides with very low water solubility (less than 0.10% (w/v)) such as com starch, rice starch, and sweet potato starch had high water solubility of approximately 45%(w/v). The gel-forming abilities with calcium ion were determined. The oxidized polysaccharides are new anionic polymers with unique structures that could have application as gums, gels, and films.

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Polarity-tuned Gel Polymer Electrolyte Coating of High-voltage LiCoO2 Cathode Materials

  • Park, Jang-Hoon;Cho, Ju-Hyun;Kim, Jong-Su;Shim, Eun-Gi;Lee, Yun-Sung;Lee, Sang-Young
    • Journal of the Korean Electrochemical Society
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    • v.14 no.2
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    • pp.117-124
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    • 2011
  • We demonstrate a new surface modification of high-voltage lithium cobalt oxide ($LiCoO_2$) cathode active materials for lithium-ion batteries. This approach is based on exploitation of a polarity-tuned gel polymer electrolyte (GPE) coating. Herein, two contrast polymers having different polarity are chosen: polyimide (PI) synthesized from thermally curing 4-component (pyromellitic dianhydride/biphenyl dianhydride/phenylenediamine/oxydianiline) polyamic acid (as a polar GPE) and ethylene-vinyl acetate copolymer (EVA) containing 12 wt% vinyl acetate repeating unit (as a less polar GPE). The strong affinity of polyamic acid for $LiCoO_2$ allows the resulting PI coating layer to present a highly-continuous surface film of nanometer thickness. On the other hand, the less polar EVA coating layer is poorly deposited onto the $LiCoO_2$, resulting in a locally agglomerated morphology with relatively high thickness. Based on the characterization of GPE coating layers, their structural difference on the electrochemical performance and thermal stability of high-voltage (herein, 4.4 V) $LiCoO_2$ is thoroughly investigated. In comparison to the EVA coating layer, the PI coating layer is effective in preventing the direct exposure of $LiCoO_2$ to liquid electrolyte, which thus plays a viable role in improving the high-voltage cell performance and mitigating the interfacial exothermic reaction between the charged $LiCoO_2$ and liquid electrolytes.

Purification of Angiogenin from Bovine Milk (우유로부터 Angiogenin의 정제)

  • Nam, M.S.;Bae, H.C.;Park, C.S.
    • Journal of Animal Science and Technology
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    • v.46 no.1
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    • pp.77-82
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    • 2004
  • This study was carried out to establish the purification protocol of angiogenin(ANG) from bovine milk. The purification of ANG from bovine milk was performed by using cation chromatography, high-performance liquid chromatography and gel-filtration. We obtained the ANG protein have the molecular weight of about 14 kD by SDS-PAGE analysis. This protein was confirmed as ANG by Nlb-terminal sequence analysis of the first 15 amino acids. Identified amino acids revealed the protein to be identical to that previously reported for bovine ANG.

Microstructure and Electrical Properties of Vanadium-doped ${Bi_4}{Ti_3}{O_{12}}$ Thin Films Prepared by Sol-gel Method (졸-겔법으로 성장시킨 바나듐이 도핑된 ${Bi_4}{Ti_3}{O_{12}}$ 박막의 미세구조 및 전기적 특성)

  • Kim, Jong-Guk;Kim, Sang-Su;Choe, Eun-Gyeong;Kim, Jin-Heung;Song, Tae-Gwon;Kim, In-Seong
    • Korean Journal of Materials Research
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    • v.11 no.11
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    • pp.960-964
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    • 2001
  • $Bi_{3.99}Ti_{2.97}V_{0.03}O_{12}$ (BTV) thin films with 3 mol% vanadium doping were Prepared on $Pt/Ti/SiO_2/Si$ substrate by sol-gel method. X-ray diffraction analysis indicated that single-phase layered perovskite were obtained and preferred orientation was not observed. Under the annealing temperature at $600^{\circ}C$, the surface morphology of the BTV thin films had fine-rounded particles and then changed plate-like at $650^{\circ}C$ and $700^{\circ}C$. The remanent polarization $(2P_r)$ and coercive field $(2E_c)$ of $700^{\circ}C$ annealed BTV thin film were 25 $\mu$C/cm$^2$ and 116 kV/cm, respectively. In addition, BTV thin film showed little polarization fatigue during $10_9$ switching cycles. These improved ferroelectric properties were attributed to the increased rattling space and reduced oxygen vacancies by substitution $Ti^{4+}$ ion (68 pm) with smaller $V^{5+}$ ion (59 pm). The dielectric constant and loss were measured 130 and 0.03 at 10 kHz, respectively.

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Studies on the Production of $\beta$-Galactosidase by Microorganism and its Application (Part 2) Physicochemical Properties of the Enzyme of Penicillium sp. and its Application (미생물에 의한 $\beta$-Galactosidase의 생산 및 이용에 관한 연구 (제2보) Penicillium sp.의 효소의 물리화학적 성질 및 이용)

  • 오평수;서항원;양한철
    • Microbiology and Biotechnology Letters
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    • v.9 no.4
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    • pp.213-218
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    • 1981
  • The molecular weight of the purified $\beta$-galactosidase of Penicillium sp. was estimated to be 130000 by both Sephadex G-200 gel filtration and SDS-polyacrylamide del electrophoresis. The SDS-electrophoresis gave two protein bands corresponding to the two molecular weights of 130000 and 70000. These results indicated that the enzyme consisted of two probably identical subunits which had a molecular weight of 70000. The optimum pH of the enzyme activity was 4.7 and maximum activity appeared at 5$0^{\circ}C$. The stable pH range for the enzyme was from 4.5 to 7.0. The purified $\beta$-galactosidase had no metal ion requirement for its activity or stability. The enzyme activity was inhibited by C $u^{++}$(1mM)and galactose (100mM). The hydrolysis of lactose in 5% lactose solution, pasteurized milk and 10% skim milk solution were 69.5%, 88.7% and 72.6% after 4 hr incubation at 5$0^{\circ}C$, when 10 units of $\beta$-glucosidase were used per $m\ell$ of the substrate solutions.s.

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Microstructures and Electrical Properties of Niobium-doped Bi4Ti3O12 Thin Films Fabricated by a Sol-gel Route (졸-겔 법으로 성장시킨 Nb가 첨가된 Bi4Ti3O12 박막의 미세구조와 전기적 성질)

  • Kim, Sang-Su;Jang, Ki-Wan;Han, Chang-Hee;Lee, Ho-Sueb;Kim, Won-Jeong;Choi, Eun-Kyung;Park, Mun-Heum
    • Korean Journal of Materials Research
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    • v.13 no.5
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    • pp.317-322
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    • 2003
  • Bismuth layered structure ferroelectric thin films, $Bi_4$$Ti_3$$O_{12}$ / (BTO) and Nb-doped BTO (BTN) were prepared on the Pt(111)/Ti/$SiO_2$/Si(100) substrates by a sol-gel route. We investigated the Nb-doping effect on the grain orientation and ferroelectric properties. $Nb^{5+}$ ion substitution for $Ti^{4+}$ ion in perovskite layers of BTO decreased the degree of c-axis orientation and increased the remanent polarization (2Pr). The fatigue resistance of Nb-doped BTO thin film was shown to be superior to that of BTO, and the leakage current of Nb-doped BTO thin film was decreased about 1 order of magnitude compared with BTO. The improvement of ferroelectric properties with $Nb^{5+}$ doping in BTO could be attributed to the changes in space charge densities and grain orientation in the thin film.

Purification and Properties of Endo-$\beta$-1, 4-glucanase from Thermophilic Clostridium thermocellum (고온성 Clostridium thermocellum이 생산하는 Endo-$\beta$-1, 4-glucanase의 정제 및 성질)

  • 김욱한;하지홍;정기택;이용현
    • Korean Journal of Microbiology
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    • v.25 no.2
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    • pp.157-164
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    • 1987
  • A new endo-$\beta$-1, 4-glucanase was purified from the culture filtrate of thermophilic anaerobic Clostridium thermocellum. The purification procedure included two steps of ion exchange chromatography with DEAD-Sephadex A-50 and gel filtration chromatography with Sephadex G-75. Even though the 56 fold increase in CMCase specific activity was obtained, the actually recovered enzyme activity was relatively lower level of 0.7%. Judging from the two bands in SDS-polyacrylamide gel electrophoresis, the endo-$\beta$-1, 4-glucanase consists of two subunits whose M.W. are 38,000 and 58,000, respectively. The optimum pH and temperature were determined to be 5.0 and $65^{\circ}C$, respectively. The enzyme was stable up to $70^{\circ}C$, but inactivated at $80^{\circ}C$. The kinetic parameters of the separated fraction were also determined. The purified enzyme did not show any significant hydrolytic activity against the highly ordered crystalline cellulose as well as filter paper.

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Purification and Characterization of Trypsin Inhibitor from Alismatis Rhizoma (택사(Alismatis Rhizoma) trypsin inhibitor의 정제와 특성)

  • 박종옥;이인섭
    • Journal of Life Science
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    • v.12 no.2
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    • pp.151-157
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    • 2002
  • A trypsin inhibitor was isolated and purified from Azismatis Rhizoma which has been used as a galenic for diuretic and antiphlogistic. Purification was carried out by 0-80% saturated ammonium sulfate salting out, DEAE- cellulose ion exchange chromatogrphy, Sephadex G-150 gel filtration. The molecular weight of Alismatis Rhizoma trypsin inhibitor(ARTI) was estimated to be about 23,000 Da by gel filtration and SDS-PAGE, it must be monomer. ARTI was stable at 0~6$0^{\circ}C$, but at higher temperature its activity was decreased about 35%. When benzoyl-dl-arginine p-nitroanilide was used as a substrate of trypsin, half-maximal inhibition of ARTI was observed at 0.071 $\mu$M. ARTI inhibited the hydrolysis of trypsin non-competitively and Km value was 0.81 $\mu$M.