• Title/Summary/Keyword: Protein A

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Solubility, Emulsion Capacity, and Emulsion Stability of Protein Recovered from Red Crab Processing Water (홍게 가공회수 단백질의 용해도, 유화력 및 안정성)

  • Kim, Yong-Jin;Sin, Tae-Seon;O, Hun-Il
    • The Korean Journal of Food And Nutrition
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    • v.9 no.3
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    • pp.319-324
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    • 1996
  • The functional properties of protein recovered from red crab (Chitinonecetes opiiie) processing in water (RCP) were examined and compared with those of soybean protein isolate at pH 2~10 in water and NaCl solu5ion. The solubilities of RCP and SPI were miniumu at pH 4, the isoelectric point and increased significantly at lower or higher than pH 4. Solubilities in NaCl solution for both proteins decreased with incr NaCl concentration increase at all pH ranges. Emulsion capacity for both proteins was also minimum at pH 4 and increased as protein concentration increased from 2 to 6%. Emulsion capacity of RCP was higher than these of SPI at pH 6∼10 and all protein concentrations. Emulsion stability showed a similar trend to that of emulsion capacity. RCP had higher oft absorption capacity and lower water absorption capacity than SPI.

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Novel Purification Method of Kv 4.2 Potassium Channel from Rat Brain Membrane

  • Park, Sung-Soo
    • Biomedical Science Letters
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    • v.18 no.2
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    • pp.96-103
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    • 2012
  • Kv 4.2 ion channel protein has an ability to open at subthreshold membrane potentials and to recover quickly from inactivation. That is very important for neuronal signal transmission in vertebrate brain. In order to purify Kv 4.2 protein, the novel purification methods were experimented. The purification procedure utilized chromatography on DE-52 ion exchange column and affinity chromatography on a WGA-Sepharose 4B, and Kv 4.2 affinity column chromatography. It was found that 0.5% (wt./vol.) Triton X-100 detergent in lysis buffer worked well for Kv 4.2 protein solubilization from rat brain membrane. Protein quantitative determination was conducted by BCA method at 562 nm for each purification step to avoid determination interference of protein at 280 nm by detergent. The confirmation of Kv 4.2 existence and amount is performed using by SDS-PAGE/immunoblotting or 96-well dot blotting. The Kv 4.2 without interacting protein that contains carbohydrate, was purified from novel biochemical 3-steps purification method for further research.

Microencapsulation Methods for Delivery of Protein Drugs

  • Yoon Yeo;Namjin Baek;Park, Kinam
    • Biotechnology and Bioprocess Engineering:BBE
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    • v.6 no.4
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    • pp.212-230
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    • 2001
  • Recent advances in recombinant DNA technology have resulted in development of many new protein drugs. Due to the unique properties of protein druges, they have to be delivered by parenteral injection Although delivery of protein drugs by other routes, such as pulmonary and nasal routes, has shown some promises, to date most protein drugs are administered by par-enteral routs. For long-term delivery of protein drugs by parenteral administration, they have been formulated into biodegradable microspheres. A number of microencapsulation methods have been developed, and the currently used microencapsulation methods are reviewed here, The microen-capsulation methods have been divided based on the method used. They are: solvent evapora-tion/extraction; phase separation (coacervation);spray drying; ionotropic gelation/polyelectrolyte complexation; interfacial polyumerization and supercritical fluid precipitation. Each method is de-scribed fro its applications, advantages, and limitations.

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NMR Studies on Transient Protein Complexes: Perspectives

  • Suh, Jeong-Yong;Yu, Tae-Kyung;Yun, Young-Joo;Lee, Ko On
    • Journal of the Korean Magnetic Resonance Society
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    • v.18 no.1
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    • pp.1-4
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    • 2014
  • It is generally understood that protein-protein interactions proceed via transient encounter complexes that rapidly evolve into the functional stereospecific complex. Direct detection and characterization of the encounter complexes, however, been difficult due to their low population and short lifetimes. Recent application of NMR paramagnetic relaxation enhancement first visualized the structures of the encounter complex ensemble, and allowed the characterization of their physicochemical properties. Further, rational protein mutations that perturbed the encounter complex formation provided a clue to the target search pathway during protein-protein association. Understanding the structure and dynamics of encounter complexes will provide useful information on the mechanism of protein association.

A comparison of detection capabilities of anti-IgG immobilizedby protein G and NHS (Protein G와 NHS를 이용하여 고정한 anti-IgG의 검출 성능 비교)

  • Sin, Eun-Jung;Sohn, Young-Ho;Sohn, Young-Soo
    • Journal of Sensor Science and Technology
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    • v.19 no.2
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    • pp.142-148
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    • 2010
  • We have compared and investigated the detection capabilities of antibody of immunoglobulin G(anti-IgG) immobilized by protein G and N-hydroxysuccinimide(NHS) at the end of the self-assembled monolayer(SAM). Surface plasmon resonance(SPR) sensor has been utilized to measure the interaction between biomolecules. After formation of the protein G and SAM, anti-IgG, bovine serum albumin(BSA) and IgG has been sequently injected. Through the reponse of the SPR, we can conclude that the protein G immobilized anti-IgG better than the SAM. In addition, IgG detection capability of the anti-IgG immobilized by the protein G showed better performance compared with that immobilized by the SAM.

Subcellular Localization of GTP Binding Protein in Stentor coeruleus

  • Park, Phun-Bum;Song, Pill-Soon
    • Journal of Photoscience
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    • v.7 no.1
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    • pp.31-34
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    • 2000
  • The heterotrichous ciliate Stentor coeruieus shows a step-up photophobic response to visible light In the previous paper, the existence of GTP-binding proteins was confirmed by using the antisera against the carboxy terminal decapeptide of transducin $\alpha$ subunit. The photoreceptor, stentorin, is localized in the pigment granule. If the immunoreactive G-protein directly interacts with the photoreceptor stentorin, the G-protein expected to be located in the pigment granule rather than plasma membrane. To elucidate the function of the immunoreactive G-protein, the localization of the G-protein in Stentor coeruleus was studied. The results suggest that this G-protein is located in the myoneme involved in the contraction and extension of the cell rather than in the pigment granule.

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Effects of Dietary Protein Levels on the Serum Lipids and Enzyme Activities of Ethanol-Administered Rats (에탄올을 투여한 흰쥐에서 식이 단백질 섭취 수준이 혈청중 지방 및 효소활성에 미치는 영향)

  • 고진복
    • Journal of Nutrition and Health
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    • v.25 no.7
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    • pp.578-585
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    • 1992
  • This study was undertaken to investigate effects of alcohol and dietary protein levels on serum lipids and enzyme activities in 15 week-old male rats given a normal diet. Rats were divided into 8 groups : control group (16% protein 16PC) and 8%(8PE) 16%(16PE) and 24% protein groups(24PE) to which was given 5% ethanol mixed into their drinking water after 4 weeks and 10 weeks. Body weight organ weight and various blood components were determined at 4 and 10 weeks. Body weight gain organ weight hemoglobin concentration and hematocrit value were not influenced by ethanol and dietary protein levels. The levels of total cholesterol HDL-cholesterol and phospholipid in serum were not affected by ethanol consumption. Serum triglyceride concen-trations after 10 weeks were significnatly increased ethanol-treated group compared with that of control group and the effect was greater in low protein group than control group. Serum ALP activity was significantly higher in 8PE group than other group but there was no influence by ethanol consumption.

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A Study on the Allergenicity of Milk Protein (우유 단백질의 Allergenicity에 관한 연구)

  • 정은자
    • The Korean Journal of Food And Nutrition
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    • v.8 no.2
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    • pp.79-87
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    • 1995
  • It is generally known that the protein of talk has allergenicity and the allerenicity Induces allergic diseases. Finding methods to reduce the allergenicity of the food and develop methods to make low allergic food is the purpose of this study. For this study, 1 tried various experimental methods : heat treatment, irradation with ultraviolet and microwaves treatment with polyphosphate, enzyme hydrolysis and PCA inhibition test using guinea pigs and degrees of hydrolysis. The results obtained are as follows. Heat treatment reduced allergenicity of milk protein. The higher the heat, the better the effect. Irradiating with ultraviolet and microwave increased both the degree of protein hydrolysis and PCA inhibition reduced the allergenicity. Ultraviolet was more effective than microwaves on milk protein. Enzyme treatment increased the degree of hydrolysis and PCA inhibition, and reduced allergenicity considerably. Neutrase was more effective than alcalase on milk protein. Adding Polyphosphate did not induced protein hydrolysis, but increased PCA inhibition and reduced allergenicity.

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SOLUTION STRUCTURE AND INTERACTION ON THE CARBOXYL- TERMINAL DOMAIN OF ESCHERICHIA COLI RNA POLYMERASE $\alpha$ SUBUNIT STUDIED BY NMR

  • Jeon, Young-Ho;Tomofumi Negishi;Masahiro Shirakawa;Toshio Yamazaki;Nobuyuki Fujita;Akira Ishihama;Yoshimasa Kyogoku
    • Proceedings of the Korean Biophysical Society Conference
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    • 1996.07a
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    • pp.11-11
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    • 1996
  • The three-dimensional structure of the carboxyl-terminal domain of the E.coli RNA polymerase $\alpha$ subunit, which is regarded as the contact site for transcription activator proteins and the promoter UP element, was determined by NMR spectroscopy. Its compact structure of four helices and two long arms enclosing its hydrophobic core shows a folding topology distinct from those of other DNA-binding proteins. (omitted)

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Drug-Biomacromolecule Interaction (III) 1-Anilinonaphthalene-8-sulfonate Binding to Bovine Serum Albumin by Fluorescence (약물과 생체 고분자간의 상호작용(III) 형광측정법에 의한 1-Anilinonaphthalene-8-sulfonate와 Bovine Serum Albumin간의 결합에 관한 연구)

  • 김종국;안해영;양지선;김양배;유병설
    • YAKHAK HOEJI
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    • v.26 no.2
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    • pp.85-90
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    • 1982
  • The binding of the 1-anilinonaphthalene-8-sulfonate(ANS) to bovine serum albumin was studied by fluorescence spectroscopy. The effect of pH, ionic strength, and protein concentration on the binding of ANS to protein were compared. The binding between ANS and protein was dependent on pH and ionic strength. It seems that both hydrophobic binding and some electrostatic forces are involved in the binding of ANS to protein. The binding constants for ANS increased with increasing protein concentration. This suggests the possibility of a sharing of one ANS molecule by more than one protein molecule at relatively high protein concentration.

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