• Food Science and Biotechnology
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• 제18권4호
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• pp.823-832
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• 2009

In recent years, special concerns have been raised about the safety assessment of foods and food ingredients derived from genetically modified organisms (GMOs). A growing number of countries establish regulations and laws for GMOs in order to allow consumers an informed choice. In this case, a lot of methods have been developed for the detection of GMOs. However, the reproducibility among methods and laboratories is still a problem. Consequently, it is still in great demand for more effective methods. In comparison with the gel electrophoresis, the capillary electrophoresis (CE) technology has some unique advantages, such as high resolution efficiency and less time consumption. Therefore, some CE-based methods have been developed for the detection of GMOs in recent years. All kinds of CE detection methods, such as ultraviolet (UV), laser induced fluorescence (LIF), and chemiluminescence (CL) detection, have been used for GMOs detection. Microchip capillary electrophoresis (MCE) methods have also been used for GMOs detection and they have shown some unique advantages.

• 대한의생명과학회지
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• 제11권4호
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• pp.493-501
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• 2005

Circadian rhythms, time on a scale of about 24 hours, are present in a number of organisms including animals, plants, and bacteria. The control of the biochemical, physiological and behavioral processes is regulated by endogenous clocks in the suprachiasmatic nucleus (SCN). At the core of this timing mechanism is molecular machinery that are present both in the brain and in the peripheral tissues throughout the body, and even in a single cultured cell. In this study, we performed two-dimensional gel electrophoresis to figure out any correlation between protein expression patterns and the requirement of two canonical clock proteins, either mPER1 or mPER2, by comparing global protein expression profiles in livers from wildtype or mPer1/mPer2 double mutant mice. We could identify several differentially expressed protein candidates with respect to time and genotypes. Further analysis of these candidate proteins in detail in vivo will lead us to the better understanding of how circadian clock functions in mammals.

• Current Research on Agriculture and Life Sciences
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• 제31권2호
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• pp.108-112
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• 2013

Nuts are one of the most common sources of allergies in individuals of all ages. In order for a particular protein to render an allergic reaction, it must resist proteolytic digestion by intestinal enzymes. In this study, three well-known allergenic nuts, almonds, cashew nuts, and peanuts, were used as samples, and enzyme digestion with Bacillus protease and porcine pepsin was tested. A proteomic approach using two-dimensional gel electrophoresis and an MS/MS analysis was applied to visualize and identify the proteins that were resistant to enzyme digestion. Among the 150 protein spots tested, 42 proteins were assigned functions. Due to the lack of genomic databases, 41% of the identified proteins were grouped as hypothetical. However, 12% of them were well-known allergens, including AraH. The remainder were grouped as storage, enzymes, and binding proteins.

• 한국동물학회지
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• 제34권3호
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• pp.394-402
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• 1991

Yolk protein-3 (YP3) was purified from the ovary of Hvpharatria cunea D. and the synthesis and fate during embryogenesis of WP3 were investisated by electrophoresis and fluorography. YP3 purified through gel slice and electrophoretic elution'was determined to have M. W. of 18 Kd and consist of one subunit. Haemolymph and fat body of male and female %were electrophoresed during vifellogenic stages to indentifv the vitellosenin in female. The result showed that there was no distinct difference in electrophoretic patterns betweerl male and female. However, tissue culture of fat body and maturing ovary indicated that YP3 was svuthesized by fat body. Aiso, vP3 in iaid eggs was maintained constant untii naut s artier oviposition and then decreased, indicating that YP3 was drastically used during late embryosenesis. However, a part of YP3 was present even in newly hatched first instar larvae.

• 약학회지
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• 제27권4호
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• pp.315-320
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• 1983

Ginseng proteins have been extracted and partially purified by the methods of ammonium sulfate fractionation, heat inactivation and Sephadex G-75 column chromatography. The final three fractions obtained (GI, GII and GIII) were subjected to paper chromatography and SDS-polyacrylamide gel electrophoresis. Molecular weights of polypeptide chains from each fraction were est-mated by the standard line obtained from the plot of electrophoretic mobilities against the logarithm of molecular weights of standard proteins. Results are as follows: 1) GI showed three protein spots and four polypeptides of which M.W. were 63,000, 60,000, 56,000, 51,000 and 34,200. 2) GII showed four protein spots and five polypeptides with their M.W. of 64,600, 56,000, 45,400, 35,800, end 25,200, 3) GIII showed three protein spots and four polypeptides with their M.W. of 66,000, 63,000, 56,000 and 22,000.

• 한국식물병리학회지
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• 제2권2호
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• pp.121-128
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• 1986

액독 TMV, Tw 333 RNA 및 외피단백질에 대한 생화학적 특성을 조사하였다. Tw333-RNA는 $2.03\times10^6$dalton의 분자량을 나타냈고, 고기조성은 guanine 25.4, adenine 29.2, cytosine 17.5, uracil 27.9mol이었다. 열처리에서 얻어진 이 RNA의 농색효과는 $25.1\%$를 나타냈고, 이때 Tm치는 $47^{\circ}C$였다. 한편 Tw 333의 외피단백질은 17,500 dalton의 분자량을 보였으며, 16종의 아미노산으로 구성된 158개의 아미노산잔기를 나타냈다. Trypsin으로 분해한 단백질은 9종의 ninhydrin 양성반응 peptide를 형성하였다. 이들 약독 TMV, Tw333-RNA 및 외피단백질의 생화학적 특성은 원주 OM계통과 전반적으로 매우 유사하였다. 그러나 고기조성, 농색효과, 아미노산조성 및 peptide map에서 약간의 차가 인정되었다.

• 한국식품과학회지
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• 제16권3호
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• pp.322-328
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• 1984

Pizopus oryzae가 생산(生産)하는 glucoamylase를 유안(硫安)및 acetone 분획(分劃)과 이온교환수지의 column chromatography에 의하여 정제(精製)하였다. 즉(卽) 조효소액(粗酵素液)을 유안분획(硫安分劃) acetone 분획(分劃), DEAE-cellulose column chromatography, CM-cellulose column chromatography에 의(依)하여 두가지형(型)의 glucoamylase를 분리정제(分離精製)하였으며 이들을 각각(各各) glucoamylase I과 II라고 하였다. Glucoamylase I과 II의 Specific activity는 각각(各各) 157.6U/mg protein (조효소액(粗酵素液)의 37.5배(倍)) 164.7U/mg protein (조효소액(粗酵素液)의 39.2배(倍)) 이었고 수율(收率)은 각각(各各) 4.3%, 3.8%이었다. Glucoamylase I과 II는 polyacrylamide disc gel electrophoresis와 SDS-polyacrylamide gel electrophoresis에 의(依)하여 각각(各各) 단일(單一)한 band를 나타내었고 이 단백질(蛋白質) band는 옥도염색(沃度染色)에 의(依)해 glucoamylase 활성(活性)을, PAS염색(染色)에 의(依)해 glycoprotein임을 확인(確認)하였다.

• 한국작물학회지
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• 제60권1호
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• pp.114-122
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• 2015

침종 기간과 침종 후 발아의 유무에 따른 단백질 발현을 이차원전기영동을 이용하여 단백질 발현양상을 확인하고 비교 분석한 결과, 침종 기간과 침종 후 발아의 유무에 따른 단백질 발현 양상은 전반적으로 매우 유사하였으며, 주요 단백질의 발현에는 차이가 없었다. 침종 기간에 따른 품종별 단백질 발현 양상은 침종 기간이 길어짐에 따라 단백질 발현정도가 점차 증가되는 것을 확인할 수 있었다. 공시품종들 중 황금콩, 단엽콩, Peking이 다른 품종들에 비하여 침종 4일후에 단백질 발현정도가 급격히 증가하는 것을 알 수 있었다. 침종 후 발아 유무에 따른 단백질 발현양상은 소수의 단백질 spot들을 제외하고는 전반적으로 모든 공시 품종들에서 발아한 종자에서의 단백질 발현정도는 미발아 종자에서보다 높게 확인되었다.

• 한국식품과학회지
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• 제5권2호
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• pp.78-83
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• 1973

선별된 Aspergillus 속의 한 균주인 S-1의 조(粗) naringin 분해효소의 정제에 관하여 검토한 결과 정제도의 관점에서 Sephadex G-200, starch gel electrophoresis, DEAE-Cellulose column chromatogram, 황산암모늄분획의 순위로 좋았으며 각 정제법에 따른 결과는 다음과 같다. 1) 조효소(粗酵素)를 starch gel electrophoresis 한 결과 단백 mg 당 naringinase 활성이 1,000 unit 로 정제되었다. 2. 단백 mg 당 0.37 unit, naringinase 활성인 조효소(粗酵素)를 황산암모늄분획한 결과 0.25포화 이하에서는 protein per mg 3 unit, 0.75포화 이하에서는 12 unit, 075포화 이상 완전포화 fraction 에서는 34 unit 로 정제되었으며 회수율로 볼때는 황산암모늄 0.75포화 이하에서 가장 좋았다. 3. Sephadex G-200에 의해 정제한 결과 protein per mg 1,337 unit 였으며 DEAE-Cellulose column chromatography 한 결과는 430 unit per protein mg 으로 정제되었다. 4. DEAE-Cellulose column chromatography 후 sephadex G-200에 의해 정제한 결과는 여지전기영동에 의해 단일 단백으로 나타났으며 이 단일 단백은 naringin 을 purunin 까지만 분해하였다.

• 대한핵의학회지
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• 제4권1호
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• pp.43-49
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• 1970

In recent years with development of immuno-electrophoresis, more acurate analysis of the serum protein became possible. However, there is few reports in the literature which investigated the changes of the immunoglobulin compared with electrophoretically fractioned serum thyroglobulin in the patients with various thyroid diseases. The purpose of this report is to investigate the changes of thyroglobulin in various thyroid diseases by the method of immuno-electrophoresis and to compare the results with.serum protein fractionated by the method of agar-gel micro-electrophoresis. Materials and Methods: Sera from 9 patients with diffuse toxic goiter, 2 nodular nontoxic goiter, 2 thyroiditis, 3 hypothy, roidism, 1 thyroid cancer, 7 cystic degeneration of the thyroid gland, and 10 normal subject were taken. All cases were confirmed by various laboratory thyroid function tests and thyroid needle biopsy. Immuno-electrophoretic analysis of the serum were performed by Scheidegger's modified micro-immuno-electrophoretic method. The antiserum was obtained from the Travenol Laboratories International, Hyland Products Division and was rabbit anti-human thyroglobulin. Microscope slide agar-gel electrophoresis for serum protein fractionation was performed at $4^{\circ}C$ using veronal buffer, pH 8.6 and ionic strength 0.05, with 54 volts and 2.8 mA for 60 minutes. The fractionated slide was stained with 0.1% thiazine red. The results were as follows: 1) Increase of immune-globulin macroglobulin (IgM), alphaglobulin, and immune-globulin A (IgA) by 95.8%, 100%, 29.2% respectively was found in the serum from various thyroid diseases. 2) Thyroglobulin fraction was found to be increased in 50%, no change in 41.7%, and no line in 8.3% with all of the various goiter patients. On the other hand, 10 normal control group showed only 2 cases of increase, 5 cases of no change and 3 cases of no line.