• Proceedings of the KSAR Conference
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• 2002.06a
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• pp.88-88
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• 2002

Erythropoietin (EPO)는 조혈작용 (erythropoiesis)을 나타내는 호르몬으로서 사람의 빈혈치료제로 사용되며, 포유통물 중 사람, 생쥐 등의 유즙 내에 혈청 EPO 와 동일한 크기로 다량으로 존재한다고 보고된 바 있다. 생쥐의 WAP promoter를 이용하여 사람의 조혈촉진제인 EPO를 유즙으로 생산하는 형질전환돼지 (새롬이)의 유즙을 분석하기 위해 SDS-PAGE와 Western blotting 을 수행하였다. 먼저, 형질전환돼지의 유즙으로부터 원심분리에 의해 지방층을 제거한 후, 16.5% polyacrylamide gel 에서 PAGE를 수행하였다. (중략)

• Korean Journal of Microbiology
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• v.27 no.4
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• pp.436-438
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• 1989

We propose a method for rapid evaluation and permanent record of sodium dodecyl sulfate polyacrylamide gel electrophoretic runs. This method is based on the photocopy process, rather than on photography and requires no extensive or expensive investment. Comparison of a print obtained through this method and a 35mm photography indicated, on a balanced gel, equal sensitivity.

• The Korean Journal of Food And Nutrition
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• v.6 no.4
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• pp.307-313
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• 1993

Bacillus cereus $\beta$-amylase was purified by Sephadex G-100 gel filtration, CM Sephadex C-50 ion exchange chromatography and CM Sephadex C-50 ion exchange rechromatography The purified enzyme showed 871 unit/mg of specific activity. The purified enzyme was identified as homogenious by disc PAGE, SDS-PAGE and analysis of reaction product. The purified enzyme showed optimum pH 7.0. optimum temperature 5$0^{\circ}C$, and was stable at 0~5$0^{\circ}C$ and at pH range of 6~10.

• Journal of Aquaculture
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• v.21 no.4
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• pp.285-293
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• 2008

Vitellogenin (Vg) is the precursor of vitellin (Vn), the major yolk protein of teleost fishes. In this study, Vg and Vn proteins of the Korean bullhead Pseudobagrus fulvidraco were isolated using gel-filtration chromatography (Sephadex-G 200 column) and anion-exchange chromatography (Mono Q HR 5/5 column), respectively. Purified Vn with an estimated molecular mass of 360 kDa by gel filtration chromatography was obtained from ovarian egg, and it was composited to one major subunit with an estimated molecular mass of 107 kDa by SDS-PAGE. In the result of western blotting, one major band was detected using antiserum against Vn (anti-Vn). These results suggested that Vn was composed of three subunits having the same molecular weight in Pseudobagrus fulvidraco. Vg was induced by estradiol-$17{\beta}$ ($E_2$) and purified from $E_2$ treated male serum. The molecular weight of whole Vg was estimated to be 450 kDa by gel filtration chromatography, and it is composed of three subunits with estimated molecular masses of 110 kDa, 125 kDa and 147 kDa as determined by SDS-PAGE. In the Ouchterlony's immunodiffusion test using anti-Vn and antiserum against female and male serum, purified Vg was detected in matured female and Ez treated male serum but not in untreated male. These results can be used in detecting estrogenic contamination of the aquatic environment.

• Journal of the Korean Society of Food Science and Nutrition
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• v.43 no.4
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• pp.557-563
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• 2014

This study was conducted to evaluate the effects of physical treatments on the antigenicity of gliadin in strong wheat flour. Strong wheat flour was treated with an autoclave (5, 10, 30, 50 min), a microwave (1, 5, 10 min), or both (10, 30, 50 min/ 5, 10 min), followed by SDS-PAGE, immunoblotting, and Ci-ELISA using anti-gliadin IgG. The results indicated that the binding ability of IgG to gliadin in strong wheat flour slightly decreased after autoclaving or autoclaving/microwaving. In particular, the binding ability was reduced to about 87% after autoclaving for 50 min and to 89% after autoclaving/microwaving (50/5 min). In addition, gliadin bands in the 50 min autoclaved group disappeared in both SDS-PAGE and immunoblotting. On the other hand, the antigenicity of gliadin was unaffected by microwaving alone. In conclusion, the results of this study suggest that autoclaving may reduce the antigenicity of gliadin in strong wheat flour.

• The Korean Journal of Zoology
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• v.33 no.4
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• pp.461-467
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• 1990

To investigate the neurological effect of acrylamide, whole brain of Intoxicated mouse induced early hindlimbs ataxia was examined by using the methods of SDS-PAGE and two-dimensional electrophoresis. In the gel patterns by SDS-PAGE, when the patterns of each group were compared relatively, there were no remakable changes but in the patterns of 2D-PAGE, some protein alterations were observed. Especially, the spots containing 20 (14,500, 5.64) and 21 (19,900, 6.78) were disappeared, and the spots 9 (31,300, 5.82), 11 (31,300, 5.36) and 19 (16,400, 5.42) showed marked decrease relatively in the case of treatment group. Among these changed spots, the spot 20 (14,500, 5.64) showed higher quantity than that of control group but several spots containing the spots 11 (31,300, 5.36), and 19(16.400, 5.42) were identical or equal to those of control In quantity in the case of recovery group. It seems that acrylamide might already inhibit the brain protein synthesis mechanism at the time of onset of distal neuropathy by participation in the protein metabolism so as to impair the brain regulation ability followed by a malfunction of mouse central nervous system (CNS) and recovery is gradually progressed with the dose and duration dependence after the cessation of acrylamide administration.

• Korean Journal of Food Science and Technology
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• v.32 no.4
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• pp.822-827
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• 2000

Gamma irradiation was applied to reduce shrimp allergy. Shrimp heat-stable protein(HSP) and shrimp protein extract were gamma-irradiated at 1, 3, 5, 7 or 10 kGy in an aqueous state (1.0 mg/mL). The changes in allergenic and antigenic properties of protein extract and HSP resulted from gamma irradiation were monitored by ELISA with mouse mAb or human patients sera and immunoblotting. Conformational changes in irradiated HSP were measured by both GPC-HPLC and SDS-PAGE. The binding ability of shrimp allergic patients IgE to irradiated protein extract or irradiated heat-stable protein was dose-dependently reduced. When measured by gel permeation chromatography and sandwich ELISA, the amount of intact heat-stable protein in the irradiated solution was reduced by gamma irradiation depending upon the applied dose. SDS-PAGE showed that the main band disappeared and new bands appeared in a higher molecular weight zone. The results provide a new possibility to use irradiation process for reducing the allergenicity of shrimp.

• Applied Biological Chemistry
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• v.43 no.4
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• pp.260-265
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• 2000

To determine the quality change of the irradiated eggs during storage, fresh shell eggs were irradiated using $^{60}Co$ at 0, 1, 5, 10, 30 kGy and stored for 30 days. The york index, color, pH, viscosity, egg weight, and SDS-PAGE profile of the irradiated eggs were examined. During storage, york index values of the irradiated eggs and the control were decreased and the increase of dose decreased yolk index. However, the yolk index values were increased temporarily at 10 kGy and 30 kGy. The yolk color had a bright yellow with increases in dose level and there was no significant change during storage. The albumen viscosities were decreased with increases in dosage and were decreased during storage. Also, the albumen pH values of the irradiated eggs were higher than that of the control and were increased during storage. The weight losses of eggs were increased during storage and there were no significant changes by dose level. SDS-PAGE profile of the egg white proteins of the shell eggs showed the change in molecular weight distribution and had aggregation pattern as well as degradation. CD and fluorescence spectroscopy study showed changes in the secondary and tertiary structure of egg white proteins by ${\gamma}-irradiation$. Therefore, this study clearly indicates that irradiation dose of eggs should be appropriate to prevent the loss of egg qualities.

• Korean Journal of Food Science and Technology
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• v.31 no.5
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• pp.1262-1267
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• 1999

Optimum reaction conditions for gel formation of rapeseed, Brassica napus, protein catalyzed by microbial TGase(transglutaminase) were evaluated by measuring breaking strength and deformation of gel. The polymerization of the protein gel was ascertained by SDS-PAGE and content of GL crosslinking$[{\varepsilon}-({\gamma}-glutamyl)lysine]$. In the reaction between rapeseed protein and TGase at $45^{\circ}C$ for 60 min, the breaking strength and deformation of the gel was the maximum at the ratio of 1 : 40 of enzyme to substrate. 10%(w/v) of rapeseed protein concentrate was optimum for gel production. The maximum breaking strength and deformation was shown at $45^{\circ}C$ The breaking strength increased linearly up to 90 min of the reaction time and remained unchanged. The breaking strength and deformation by TGase treatment was pH dependent and pH 7 was optimum for 10% rapeseed protein solution. SDS-PAGE analysis indicated that new band of highmolecular polymers were formed by the enzyme reaction, with disappearing the original bands of rapeseed protein. According to HPLC analysis. the content of GL crosslinking was increased from 0 to $7.14\;{\mu}mol/g$ gel for 90 min of the reaction time.

• Journal of Animal Science and Technology
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• v.44 no.6
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• pp.801-808
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• 2002

Proteolytic activities of some commercial milk clotting enzymes(rennet, trypsin, pepsin, papain W-40, neutrase 1.5 and protease S) in bovine skim milk containing 0.02% $CaCl_2$ were determined by measuring DH(Degree of Hydrolysis), NPN(Non Protein Nitrogen) and by comparing patterns of SDS-PAGE(Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis). The DH of microbial enzymes(neutrase 1.5 and protease S) and trypsin in bovine skim milk were higher than those of pepsin and papain W-40. The amounts of NPN in the milk treated with trypsin and the other animal enzymes(rennet and pepsin) showed the highest and lowest degrees of proteolysis, respectively. SDS-PAGE showed that trypsin and protease S hydrolyzed $\alpha$-lactalbumin and papain W-40 hydrolyzed $\beta$-lactoglobulin slightly, while neutrase 1.5 hydrolyzed both $\alpha$-lactalbumin and $\beta$-lactoglobulin after treating for 90 min. Trypsin and protease S easily hydrolyzed ${\alpha}_s$-casein and $\beta$-casein, which were not hydrolyzed by rennet. Papain W-40 hydrolyzed $\kappa$-casein more than rennet as shown in SDS-PAGE. Based on the results of the experiments, the DH and NPN of trypsin, neutrase 1.5 and protease S were shown to be higher than those of the other enzymes. The SDS-PAGE patterns of papain W-40 and neutrase 1.5 were similar with that of rennet.