• 제목/요약/키워드: affinity media

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The Influence of Social Media Affinity on Eating Attitudes and Body Dissatisfaction in Philippine Adolescents

  • Tadena, Shannen;Kang, So Ra;Kim, Shin-Jeong
    • Child Health Nursing Research
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    • 제26권1호
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    • pp.121-129
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    • 2020
  • Purpose: This study aimed to examine the influence of social media affinity on eating attitudes and body dissatisfaction among adolescents in the Philippines. Methods: The participants were 114 junior high school students enrolled in 7th to 10th grade in Cavite Province, Philippines. The collected data were analyzed in SPSS, using descriptive statistics, the independent t-test, one-way analysis of variance, Pearson correlation coefficients, and stepwise multiple linear regression. Results: The factors affecting eating attitudes were body dissatisfaction (β=-.47, p<.001), social media affinity (β=.33, p<.001) and grade (10th grade) (β=-.28, p<.001), and the factors influencing body dissatisfaction were eating attitudes (β=-.65, p<.001) and social media affinity (β=.17, p=.041). Conclusion: In order to promote healthy eating attitudes and to improve body satisfaction among Philippine adolescents, educational strategies tailored to social media users will be needed.

Affinity Chromatography를 이용한 Glucose-6-Phosphate Dehydrogenase의 신속한 정제방법 개발 (Rapid Purification of Glucose-6-Phosphate Dehydrogenase by Affinity Chromatography)

  • 이한수;임정빈
    • 미생물학회지
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    • 제21권4호
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    • pp.221-228
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    • 1983
  • Saccharomyces cerevisiae로 부터 glucose-6-phosphate dehydrogenase을 신속하고 간편하게 정제하는 과정을 affinity chromatography를 이용하여 개발하였다. 이 효소를 정제하는데 적절한 affinity medium을 조사해 본 결과, $NADP^+ -agarose$와 Affi-gel Blue(Cibacron Blue F3GA)가 Affi-gel Red(Procion Red HE-3B), AMP-agarose, ATP-agarose, 그리고 $NADP^+ -agarose$보다 유용함이 밝혀졌다. 이 두가지 affinity media에 흡착된 효소를 분리 하는데 가장 적합한 elution 조건을 조사하였는데 KCI gradient( (0-1.OM)가 효소의 순도 및 수회율을 가장 높일 수 있는 적합한 방법이었다. 특히 Affi-gel Blue를 사용할 경우, KCI gradient로 효소를 용출시키기 전에 NAD-(15mM)로NAD+에 친화역을 갖는 효소들을 제거하는 것이 enzyme의 순도를 높이는데 매우 효과적이었다. 그 결과 glucose-6-phosphate dehydrogenase를 baker's yeast로 부터 기존의 간단한 정제 과정과 affinity chromatography를 병행한 방식을 샤용하여 분리 하였는데, affinity medium으로 Affi-gel Blue를 사용했을 때는 180배 정도, NADP+-agarose를 사용했을 때는 2,000배 정도로 정제 되었다. 대량으로 glucose-6-phosphate dehydrogenase를 정제하는 경우, Affi-gel Blue를 사용하던 효소의 순도는 NADP+-agarose보다 낮으나, 효소의 회수율은 훨씬 더 높았다. 또한 G-6-P dehydrogenase에 대한 affinity medium의 capacity도 Affi-gel Blue가 NADP+-agarose보다 5배정도 높았으며 더우기 Affi-gel Blue는 여러번 반복적으로 사용될 수 있고, 그 제조 과정도 NADP+-agarose보다 간단하며 경비도 적게 들었다.

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Control of Thin Film Media Microstructure by Using Very Thin Seedlayer Material with Different Affinity for Oxygen

  • Djayaprawira, D.D.;Yoshimura, Satoru;Takahashi, Migaku
    • Journal of Magnetics
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    • 제7권3호
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    • pp.106-114
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    • 2002
  • To reduce the grain size and the media noise in a typical CrMo/CoCrPtB longitudinal media, a sputtering process which includes the exposure of oxygen onto the surface of CrW$_x$ (x=0, 25, 50, 75, 100 at.%) and CrTi$_{15}$ seedlayers with the thickness of 0.5 nm have been utilized. The main results are: (1) the media grain size and the media noise are reduced when using CrW$_x$ (x=0, 25, 50 at.%) seedlayers, and not reduced when using CrTils or CrW$_x$ (x=75, 100 at.%) seedlayers, (2) AES and RHEED results suggest that W seedlayer, which has the highest melting point, forms layer-like film with very small and dense island grain, due to its high free surface energy and low mobility. On the other hand, CrW$_{50}$ and Cr seedlayers, which have lower melting point than W seedlayer, form island film, (3) to effectively reduce the media grain size and improve the media signal to noise ratio, it is essential to utilize a very thin Cr-based seedlayer with high affinity for oxygen and which forms island-like structure, such as CrW$_{50}$ seedlayer.

항생물질 생산 방선균의 역가 개량에 관하여 (Improvement of Antibiotic-Producing Streptomyces)

  • 민경희
    • 미생물학회지
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    • 제14권4호
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    • pp.176-185
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    • 1976
  • An improved procedure for the rapid purification of glucose-6-phosphate dehydrogenase from extracts of Saccharomyces cerevisiae was developed by using affinity chromatography. Among six affinty media tested, NADP$^{+}$-agarose and Affi-gel Blue were more effective than others (i.e., Affi-gel Red, AMP-agarose, ATP-agarose, and NAD$^{+}$-agarose). Conditions to desorb the enzyme bound to the affinity media were examined to increase the purity as well as yield. The best result was obtained when the column was developed with a linear gradient of KCl (0-1.0M). In case of Affi-gel Blue, introduction of NAD$^{+}$ (15mM) washing step prior to the salt gradient was most effective to remove NAD$^{+}$-binding proteins. For a large scale preparation of G-6-P dehydrogenase higher recovery was obtained by Affi-gel Blue than NADP$^{+}$-agarose, however, the purity of the enzyme was decreased by 10 times if the former was used as the affinity medium. The capacity of Affi-gel Blue for G-6-P dehydrogenase was found to be 5 times higher than that of NADP$^{+}$-agarose. Furthermore Affi-gel Blue could be reused repeatedly and its preparation is relatively easier and less expensive than NADP$^{+}$-agarose.X> +/-agarose.

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항체를 이용한 Endoinulinase 생산 곰팡이의 검색 (Screening of the Endoinulinase-producing Fungi by Using Antibody)

  • 이선희;김미경;정미선;정용섭;엄태붕
    • 한국미생물·생명공학회지
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    • 제21권1호
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    • pp.18-22
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    • 1993
  • Oligofructo당 생산에 이용될 수있는 endoinulinase 분석방법은 그 균주가 endo- 및 exoinulinase를 함께 내는 경우, 일반적인 환원당 분석법으로는 정량하기가 어려워진다. 이 실험에서는 endoinulinase만을 선택적으로 정량하기 위한 하나의 방법으로써 항체 분석법을 이용하였다. Aspergillus niger ATCC 16882 조효소액을 CM-DEAE ion exchange chromatography, pI 2.5-5에서 preparative isoelectric focusing, HPLC gel filtration을 통해 순수하게 endoinulinase에 대한 항체를 얻었다.DEAE-ion exchange 및 protein A에서 정제된 이항체는 immunoassay 한 결과, exoinulinase 가 아닌 endoinulinase와 만 특이하게 반응하였고, immuno affinity chromatography 결과들은 배양액 중의 다른 단백질과 반응하지 않음이 확인되었다. 이눌린을 유일한 탄소원으로 한 배지에서 자란 1200여개의 야생균주들로부터 배양 특성이 우수한 균주를 1차로 선별하고 이 균주들의 endoinulinase 함량을 rocket immunoassay를 통하여 조사하였다. 이 중 1개의 균주는 Novozyme의 ATCC 1688와 비교할만한 정도의 endoinulinase를 배양액 중에 분비함을 확임할 수 있었다.

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Purification of Deoxycytidine Kinase from Various Human Leukemic Cells by End-product Analog Affinity Chromatography

  • Kim, Min-Young
    • BMB Reports
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    • 제28권4호
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    • pp.281-289
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    • 1995
  • Homogeneous human deoxycytidine kinase was purified in one step from a variety of spontaneous human leukemic cells (T-ALL, B-ALL, B-CLL, AML, CML), and from cultured T-lymphoblast cells (MOLT-4) using the newly developed affinity medium, $dCp_4$-Sepharose. Starting with an ammonium sulfate fraction, purification was achieved in one step with the kinase being eluted from a column by the end product inhibitor, dCTP. The purified deoxycytidine kinase from T-ALL cells phosphorylated deoxyadenosine and deoxyguanosine, as well as deoxycytidine. The enzyme purified from T-ALL and B-CLL cells yielded one major band with a molecular weight of 52 kDa determined by SDS-polyacrylamide gel electrophoresis. AML and CML cells yielded one 52 kDa band and an extra band of 30 kDa molecular weight. On the other hand, B-ALL and MOLT-4 cells showed a low molecular weight band of 30 kDa only. However, the electrophoretic mobilities of enzymatic activity in 12% non-denaturing gels were identical for the dCyd kinase from all different kinds of leukemic cell lines, except that the B-ALL, B-CLL, and MOLT-4 cell preparations had an extra minor peak, all at the same position. dAdo and dCyd phosphorylating activities comigrated indicating that these activities are all associated with the same protein. Two new methods, a disk implantation method and a nitrocellulose powder method were used with a small amount of enzyme protein to raise polyclonal antibodies against dCyd kinase purified from T-ALL cells.

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Biochemical Application of IgG Fc-binding peptide: From Biochip to Targeted Nano Carrier

  • Chung, Sang Jeon
    • 한국진공학회:학술대회논문집
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    • 한국진공학회 2013년도 제44회 동계 정기학술대회 초록집
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    • pp.84-84
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    • 2013
  • FcBP consisting of 13 amino acids specifically binds to Immunoglobulin G Fc domain. Initially, we utilized this peptide for preparation of antibody chip as a PEG composite for enhanced solubility. After then, the peptide conjugate was immobilized on agarose resin, resulting in highly efficient affinity column for antibody purification. The efficiency was comparable to commercial Protein A column. Recently, this peptide was conjugated with cell penetratingpeptide (CPP) on a backbone of GFP, affording antibody transducer, which carries antibody into live cells by simple mixing of antibody and the transducer in cell culture media. Antibody transduction into cells was monitored by live cell imaging. More recently, the FcBP was fused to ferritin cage, which consists of 24 ferritin protein molecules. The FcBP-ferritin cage showed greatly increased binding affinity to human IgG. Its binding was analyzed by QCM and SPR analysis. Finally, it was selectively delivered by Herceptin to SKBR3, a breast cancer cell, over MCF10A, non-tumorigenic cells.

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재조합 Escherichia coli 시스템을 이용한 폐흡충 cystein proteinase의 생산 연구

  • 홍성희;이길환;전희진;황현아;박성렬;황영보;박현
    • 한국생물공학회:학술대회논문집
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    • 한국생물공학회 2000년도 추계학술발표대회 및 bio-venture fair
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    • pp.651-654
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    • 2000
  • 본 연구에서는 재조합 E. coli 시스템에 의한 재조합 cystein proteinase의 대량 생산을 위하여 4L 회분 배양 및 최적 지수 생장기에서의 IPTG- induction을 연속적으로 실시하였다. 발현된 rPwCP1 양은 진탕 배양 시스템에서의 결과와 비교해 볼때 현저하게 향상되었음을 알 수 있었으며, 더불어 metal affinity chromatography 방법으로 처리하여 전기영동을 수행한 결과, 목적 재조합 단백질만을 정제 및 농축시킬 수 있음이 확인되었다.

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Preparation of High-Purity Urokinase Using Single-Step Hydrophobic Interaction Chromatography with p-Aminobenzamidine Ligand

  • Cao, Xue-Jun;Zhou, Jian-Hua;Huang, Zhen-Hui;Wu, Xing-Yan;Hur, Byung-Ki
    • Journal of Microbiology and Biotechnology
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    • 제12권2호
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    • pp.196-203
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    • 2002
  • A novel process for urokinase purification was studied using p-aminobenzamidine as the ligand and sepharose 4B as the matrix. The adsorption, washing, and elution conditions were optimized by an unusual method. An adsorption buffer containing 2.5 M NaCl and $1\%$ Tween 80 facilitated the adsorption of urokinase on the affinity media and prevented contaminants from binding to the p-aminobenzamidine affinity gel. It was found that $5\%$ Tween 80 removed most of the contaminants from the affinity column. A 0.2 M glycine elution buffer containing 0.5 M NaCl (pH 3.0) was found to have a strong elution ability with a high recovery and purity of urokinase. A crude urokinase material of231 IU/mg protein from human urine was purified to 124,300 IU/mg protein with a purification factor of 538 and yield of $86.7\%$. As a result, a high purity urokinase was obtained with only a single affinity chromatography step. The purification process was successfully scaled-up to a 2-1 chromatography column. The resulting urokinase eluate could be directly lyophilized, thereby complying with Chinese pharmacopoeia (1995 version) standards.